Enzyme Nomenclature

Continued from EC 1.7 and EC 1.8

EC 1.9 to EC 1.12

Sections

EC 1.9 Acting on other nitrogenous compounds as donors
EC 1.9.3 With oxygen as acceptor
EC 1.9.6 With a nitrogenous compound as acceptor
EC 1.9.99 With unknown physiological acceptors

EC 1.10 Acting on diphenols and related substances as donors
EC 1.10.1 With NAD+ or NADP+ as acceptor
EC 1.10.2 With a cytochrome as acceptor
EC 1.10.3 With oxygen as acceptor
EC 1.10.5 With a quinone or related compound as acceptor
EC 1.10.99 With unknown physiological acceptors

EC 1.11 Acting on a peroxide as donors
EC 1.11.1 Peroxidases

EC 1.11.2 With H2O2 as acceptor, one oxygen atom of which is incorporated into the product

EC 1.12 Acting on hydrogen as donors
EC 1.12.1 With NAD+ or NADP+ as acceptor
EC 1.12.2 With a cytochrome as acceptor
EC 1.12.5 With a quinone or similar compound as acceptor
EC 1.12.7 With an iron-sulfur protein as acceptor
EC 1.12.98 With other, known, physiological acceptors
EC 1.12.99 With unnown physiological acceptors


EC 1.9 ACTING ON A HEME GROUP OF DONORS

EC 1.9.3 With oxygen as acceptor

Contents

EC 1.9.3.1 cytochrome-c oxidase
EC 1.9.3.2 included with EC 1.7.2.1


EC 1.9.3.1

Accepted name: cytochrome-c oxidase

Reaction: 4 ferrocytochrome c + O2 + 4 H+= 4 ferricytochrome c + 2 H2O

Other name(s): cytochrome oxidase; cytochrome a3; cytochrome aa3; Warburg's respiratory enzyme; indophenol oxidase; indophenolase; complex IV (mitochondrial electron transport); ferrocytochrome c oxidase; NADH cytochrome c oxidase

Systematic name: ferrocytochrome-c:oxygen oxidoreductase

Comments: A cytochrome of the a type containing copper. The reduction of O2 to water is accompanied by the extrusion of four protons from the intramitochondrial compartment. Several bacteria appear to contain analogous oxidases.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9001-16-5

References:

1. Keilin, D. and Hartree, E.F. Cytochrome oxidase. Proc. R. Soc. Lond. B Biol. Sci. 125 (1938) 171-186.

2. Keilin, D. and Hartree, E.F. Cytochrome and cytochrome oxidase. Proc. R. Soc. Lond. B Biol. Sci. 127 (1939) 167-191.

3. Wainio, W.W., Eichel, B. and Gould, A. Ion and pH optimum for the oxidation of ferrocytochrome c by cytochrome c oxidase in air. J. Biol. Chem. 235 (1960) 1521-1525.

4. Yonetani, T. Studies on cytochrome oxidase. II. Steady state properties.J. Biol. Chem. 235 (1960) 3138-3243.

5. Yonetani, T.Studies on cytochrome oxidase. III. Improved purification and some properties. J. Biol. Chem. 236 (1961) 1680-1688.

[EC 1.9.3.1 created 1961, modified 2000]

[EC 1.9.3.2 Transferred entry: now included with EC 1.7.2.1, nitrite reductase (NO-forming) (EC 1.9.3.2 created 1965, deleted 2002)]


EC 1.9.6 With a nitrogenous group as acceptor

EC 1.9.6.1

Accepted name: nitrate reductase (cytochrome)

Reaction: 2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite

Other name(s): respiratory nitrate reductase; benzyl viologen-nitrate reductase

Systematic name: ferrocytochrome:nitrate oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 9029-42-9

References:

1. Sadana, J.C. and McElroy, W.D.Nitrate reductase from Achromobacter fischeri. Purification and properties: function of flavins and cytochrome. Arch. Biochem. Biophys. 67 (1957) 16-34. [PMID: 13412117]

[EC 1.9.6.1 created 1961]


EC 1.9.98 With other, known, physiological acceptors

EC 1.9.98.1

Accepted name: iron—cytochrome-c reductase

Reaction: ferrocytochrome c + Fe3+ = ferricytochrome c + Fe2+

Other name(s): iron-cytochrome c reductase

Systematic name: ferrocytochrome-c:Fe3+ oxidoreductase

Comments: An iron protein.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Yates, M.G. and Nason, A. Electron transport systems of the chemoautotroph Ferrobacillus ferrooxidans. II. Purification and properties of a heat-labile iron-cytochrome c reductase. J. Biol. Chem. 241 (1966) 4872-4880. [PMID: 4288725]

[EC 1.9.98.1 created 1972 as EC 1.9.99.1, transferred 2014 to EC 1.9.98.1]


EC 1.9.99 With unknown physiological acceptors

[EC 1.9.99.1 Transferred entry: iron—cytochrome-c reductase. Now EC 1.9.98.1, iron—cytochrome-c reductase (EC 1.9.99.1 created 1972, deleted 2014)]


EC 1.10 ACTING ON DIPHENOLS AND RELATED SUBSTANCES AS DONORS

Sections

EC 1.10.1 With NAD+ or NADP+ as acceptor
EC 1.10.2 With a cytochrome as acceptor
EC 1.10.3 With oxygen as acceptor
EC 1.10.5 With a quinone or related compound as acceptor
EC 1.10.99 With other acceptors


EC 1.10.1 With NAD+ or NADP+ as acceptor

EC 1.10.1.1

Accepted name: trans-acenaphthene-1,2-diol dehydrogenase

Reaction: (±)-trans-acenaphthene-1,2-diol + 2 NADP+ = acenaphthenequinone + 2 NADPH + 2 H+

Other name(s): trans-1,2-acenaphthenediol dehydrogenase

Systematic name: (±)-trans-acenaphthene-1,2-diol:NADP+ oxidoreductase

Comments: Some preparations also utilize NAD+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 51901-21-4

References:

1. Hopkins, R.P., Drummond, E.C. and Callaghan, P. Dehydrogenation of trans-acenaphthene-1,2-diol by liver cytosol preparations. Biochem. Soc. Trans. 1 (1973) 989-991.

[EC 1.10.1.1 created 1976]


EC 1.10.2 With a cytochrome as acceptor

Contents

EC 1.10.2.1 L-ascorbate—cytochrome-b5 reductase
EC 1.10.2.2 quinol—cytochrome-c reductase
EC 1.10.2.1

Accepted name: L-ascorbate—cytochrome-b5 reductase

Reaction: L-ascorbate + ferricytochrome b5 = monodehydroascorbate + ferrocytochrome b5 + H+

Other name(s): ascorbate-cytochrome b5 reductase

Systematic name: L-ascorbate:ferricytochrome-b5 oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37237-57-3

References:

1. Everling, F.C., Weis, W. and Staudinger, H. Kinetische Untersuchungen an einer Ascorbat: ferricytochrom b5-Oxidoreduktase (EC 1.1.2.?). Hoppe-Seyler's Z. Physiol. Chem. 350 (1969) 1485-1492. [PMID: 5363650]

[EC 1.10.2.1 created 1972, modified 2000]

EC 1.10.2.2

Accepted name: quinol—cytochrome-c reductase

Reaction: quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+

Other name(s): ubiquinol—cytochrome-c reductase; coenzyme Q-cytochrome c reductase; dihydrocoenzyme Q-cytochrome c reductase; reduced ubiquinone-cytochrome c reductase; complex III (mitochondrial electron transport); ubiquinone-cytochrome c reductase; ubiquinol-cytochrome c oxidoreductase; reduced coenzyme Q-cytochrome c reductase; ubiquinone-cytochrome c oxidoreductase; reduced ubiquinone-cytochrome c oxidoreductase; mitochondrial electron transport complex III; ubiquinol-cytochrome c-2 oxidoreductase; ubiquinone-cytochrome b-c1 oxidoreductase; ubiquinol-cytochrome c2 reductase; ubiquinol-cytochrome c1 oxidoreductase; CoQH2-cytochrome c oxidoreductase; ubihydroquinol:cytochrome c oxidoreductase; coenzyme QH2-cytochrome c reductase; QH2:cytochrome c oxidoreductase; ubiquinol:ferricytochrome-c oxidoreductase

Systematic name: quinol:ferricytochrome-c oxidoreductase

Comments: The enzyme, often referred to as the cytochrome bc1 complex or complex III, is the third complex in the electron transport chain. It is present in the mitochondria of all aerobic eukaryotes and in the inner membranes of most bacteria. The mammalian enzyme contains cytochromes b-562, b-566 and c1, and a 2-iron ferredoxin. Depending on the organism and physiological conditions, the enzyme extrudes either two or four protons from the cytoplasmic to the non-cytoplasmic compartment (cf. EC 1.6.99.3, NADH dehydrogenase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9027-03-6

References:

1. Marres, C.A.M. and Slater, E.C. Polypeptide composition of purified QH2:cytochrome c oxidoreductase from beef-heart mitochondria. Biochim. Biophys. Acta 462 (1977) 531-548. [PMID: 597492]

2. Rieske, J.S. Composition, structure, and function of complex III of the respiratory chain. Biochim. Biophys. Acta 456 (1976) 195-247. [PMID: 788795]

3. Wikström, M., Krab, K. and Saraste, M. Proton-translocating cytochrome complexes. Annu. Rev. Biochem. 50 (1981) 623-655. [PMID: 6267990]

4. Sone, N., Tsuchiya, N., Inoue, M. and Noguchi, S. Bacillus stearothermophilus qcr operon encoding rieske FeS protein, cytochrome b6, and a novel-type cytochrome c1 of quinol-cytochrome c reductase. J. Biol. Chem. 271 (1996) 12457-12462. [PMID: 8647852]

5. Yu, J. and Le Brun, N.E. Studies of the cytochrome subunits of menaquinone:cytochrome c reductase (bc complex) of Bacillus subtilis. Evidence for the covalent attachment of heme to the cytochrome b subunit. J. Biol. Chem. 273 (1998) 8860-8866. [PMID: 9535866]

6. Elbehti, A., Nitschke, W., Tron, P., Michel, C. and Lemesle-Meunier, D. Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes. I. Characterization of the cytochrome bc1-type complex of the acidophilic ferrous ion-oxidizing bacterium Thiobacillus ferrooxidans. J. Biol. Chem. 274 (1999) 16760-16765. [PMID: 10358017]

[EC 1.10.2.2 created 1978, modified 2013]


EC 1.10.3 With oxygen as acceptor

Contents

EC 1.10.3.1 catechol oxidase
EC 1.10.3.2 laccase
EC 1.10.3.3 L-ascorbate oxidase
EC 1.10.3.4 o-aminophenol oxidase
EC 1.10.3.5 3-hydroxyanthranilate oxidase
EC 1.10.3.6 rifamycin-B oxidase
EC 1.10.3.7 now EC 1.21.3.4
EC 1.10.3.8 now EC 1.21.3.5
EC 1.10.3.9 photosystem II
EC 1.10.3.10 ubiquinol oxidase (H+-transporting)
EC 1.10.3.11 ubiquinol oxidase (non-electrogenic)
EC 1.10.3.12 menaquinol oxidase (H+-transporting)
EC 1.10.3.13 caldariellaquinol oxidase (H+-transporting)
EC 1.10.3.14 ubiquinol oxidase (electrogenic, non H+-transporting)
EC 1.10.3.15 grixazone synthase
EC 1.10.3.16 dihydrophenazinedicarboxylate synthase

EC 1.10.3.1

Accepted name: catechol oxidase

Reaction: 2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O

Other name(s): diphenol oxidase; o-diphenolase; phenolase; polyphenol oxidase; tyrosinase; pyrocatechol oxidase; Dopa oxidase; catecholase; o-diphenol:oxygen oxidoreductase; o-diphenol oxidoreductase

Systematic name: 1,2-benzenediol:oxygen oxidoreductase

Comments: A type 3 copper protein that catalyses exclusively the oxidation of catechols (i.e., o-diphenols) to the corresponding o-quinones. The enzyme also acts on a variety of substituted catechols. It is different from tyrosinase, EC 1.14.18.1 monophenol monooxygenase, which can catalyse both the monooxygenation of monophenols and the oxidation of catechols.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9002-10-2

References:

1. Brown, F.C. and Ward, D.N. Preparation of a soluble mammalian tyrosinase. J. Am. Chem. Soc. 79 (1957) 2647-2648.

2. Dawson, C.R. and Tarpley, W.B. The copper oxidases. In: Sumner, J.B. and Myrbäck, K. (Eds.), The Enzymes, 1st ed., vol. 2, Academic Press, New York, 1951, p. 454-498.

3. Gregory, R.P.F. and Bendall, D.S. The purification and some properties of the polyphenol oxidse from tea (Camellia sinensis L.). Biochem. J. 101 (1966) 569-581.

4. Mason, H.S. Structures and functions of the phenolase complex. Nature (Lond.) 177 (1956) 79-81.

5. Mayer, A.M. and Harel, E. Polyphenol oxidases in plants. Phytochemistry 18 (1979) 193-215.

6. Patil, S.S. and Zucker, M. Potato phenolases. Purification and properties. J. Biol. Chem. 240 (1965) 3938-3943. [PMID: 5842066]

7. Pomerantz, S.H. 3,4-Dihydroxy-L-phenylalanine as the tyrosinase cofactor. Occurrence in melanoma and binding constant. J. Biol. Chem. 242 (1967) 5308-5314. [PMID: 4965136]

8. Robb, D.A. `Tyrosinase. In: Lontie, R. (Ed.), Copper Proteins and Copper Enzymes, vol. 2, CRC Press, Boca Raton, FL, 1984, p. 207-240.

9. Gerdemann, C., Eicken, C. and Krebs, B. The crystal structure of catechol oxidase: new insight into the function of type-3 copper proteins. Acc. Chem. Res. 35 (2002) 183–191. [PMID: 11900522]

[EC 1.10.3.1 created 1961, deleted 1972, reinstated 1978]

EC 1.10.3.2

Accepted name: laccase

Reaction: 4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O

Other name(s): urishiol oxidase; urushiol oxidase; p-diphenol oxidase

Systematic name: benzenediol:oxygen oxidoreductase

Comments: A group of multi-copper proteins of low specificity acting on both o- and p-quinols, and often acting also on aminophenols and phenylenediamine. The semiquinone may react further either enzymically or non-enzymically.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 80498-15-3

References:

1. Dawson, C.R. and Tarpley, W.B. The copper oxidases. In: Sumner, J.B. and Myrbäck, K. (Eds.), The Enzymes, 1st ed., vol. 2, Academic Press, New York, 1951, p. 454-498.

2. Keilin, D. and Mann, T. Laccase, a blue copper-protein oxidase from the latex of Rhus succedanea. Nature (Lond.) 143 (1939) 23-24.

3. Malmström, B.G., Andréasson, L.-E. and Reinhammar, B. Copper-containing oxidases and superoxide dismutase. In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 12, Academic Press, New York, 1975, p. 507-579.

4. Mayer, A.M. and Harel, E. Polyphenol oxidases in plants. Phytochemistry 18 (1979) 193-215.

5. Nakamura, T. Purification and physico-chemical properties of laccase. Biochim. Biophys. Acta 30 (1958) 44-52.

6. Nakamura, T. Stoichiometric studies on the action of laccase. Biochim. Biophys. Acta 30 (1958) 538-542.

7. Peisach, J. and Levine, W.G. A comparison of the enzymic activities of pig ceruloplasmin and Rhus vernicifera laccase. J. Biol. Chem. 240 (1965) 2284-2289.

8. Reinhammar, B. and Malmström, B.G. "Blue" copper-containing oxidases. In: Spiro, T.G. (Ed.), Copper Proteins, Wiley, New York, 1981, p. 109-149.

[EC 1.10.3.2 created 1961, deleted 1972, reinstated 1978]

EC 1.10.3.3

Accepted name: L-ascorbate oxidase

Reaction: 4 L-ascorbate + O2 = 4 monodehydroascorbate + 2 H2O

Other name(s): ascorbase; ascorbic acid oxidase; ascorbate oxidase; ascorbic oxidase; ascorbate dehydrogenase; L-ascorbic acid oxidase; AAO; L-ascorbate:O2 oxidoreductase; AA oxidase

Systematic name: L-ascorbate:oxygen oxidoreductase

Comments: A multicopper protein.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-44-1

References:

1. Yamazaki, I. and Piette, L.H. Mechanism of free radical formation and disappearance during the ascorbic acid oxidase and peroxidase reactions. Biochim. Biophys. Acta 50 (1961) 62-69. [PMID: 13787201]

2. Stark, G.R. and Dawson, C.R. Ascorbic acid oxidase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 297-311.

3. Messerschmidt, A., Ladenstein, R., Huber, R., Bolognesi, M., Avigliano, L., Petruzzelli, R., Rossi, A. and Finazzi-Agro, A. Refined crystal structure of ascorbate oxidase at 1.9 Å resolution. J. Mol. Biol. 224 (1992) 179-205. [PMID: 1548698]

[EC 1.10.3.3 created 1961, modified 2011]

EC 1.10.3.4

Reaction: 4 2-aminophenol + 3 O2 = 2 2-aminophenoxazin-3-one + 6 H2O

For diagram click here.

Glossary: 2-aminophenoxazin-3-one = isophenoxazine

Other name(s): isophenoxazine synthase; o-aminophenol:O2 oxidoreductase; 2-aminophenol:O2 oxidoreductase

Systematic name: 2-aminophenol:oxygen oxidoreductase

Comments: A flavoprotein which catalyses a 6-electron oxidation. The enzyme from the plant Tecoma stans requires Mn2+ and FAD [1] whereas the fungus Pycnoporus coccineus requires Mn2+ and riboflavin 5′-phosphate [2], the bacteria Streptomyces antibioticus requires Cu2+ [4] and the plant Bauhenia monandra does not require any co-factors [3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9013-85-8

References:

1. Nair, P.M. and Vaidynathan, C.S. Isophenoxazine synthase. Biochim. Biophys. Acta 81 (1964) 507-516.

2. Nair, P.M. and Vining, L.C. Isophenoxazine synthase apoenzyme from Pycnoporus coccineus. Biochim. Biophys. Acta 96 (1965) 318-327. [PMID: 14298835]

3. Rao, P.V.S. and Vaidyanathan, C.S. Studies on the metabolism of o-aminophenol. Purification and properties of isophenoxazine synthase from Bauhenia monandra. Arch. Biochem. Biophys. 118 (1967) 388-394. [PMID: 4166439]

4. Barry, C.E., 3rd, Nayar, P.G. and Begley, T.P. Phenoxazinone synthase: mechanism for the formation of the phenoxazinone chromophore of actinomycin. Biochemistry 28 (1989) 6323-6333. [PMID: 2477054]

[EC 1.10.3.4 created 1972, modified 2006]

EC 1.10.3.5

Accepted name: 3-hydroxyanthranilate oxidase

Reaction: 3-hydroxyanthranilate + O2 = 6-imino-5-oxocyclohexa-1,3-dienecarboxylate + H2O2

Other name(s): 3-hydroxyanthranilic acid oxidase

Systematic name: 3-hydroxyanthranilate:oxygen oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-53-4

References:

1. Morgan, L.R.,Jr., Weimorts, D.M. and Aubert, C.C. Oxidation of 3-hydroxyanthranilic acid by a soluble liver fraction from poikilothermic vertebrates. Biochim. Biophys. Acta 100 (1965) 393-402.

[EC 1.10.3.5 created 1972]

EC 1.10.3.6

Accepted name: rifamycin-B oxidase

Reaction: rifamycin B + O2 = rifamycin O + H2O2

Other name(s): rifamycin B oxidase

Systematic name: rifamycin-B:oxygen oxidoreductase

Comments: Acts also on benzene-1,4-diol and, more slowly, on some other p-quinols. Not identical with EC 1.10.3.1 (catechol oxidase), EC 1.10.3.2 (laccase), EC 1.10.3.4 (o-aminophenol oxidase) or EC 1.10.3.5 (3-hydroxyanthranilate oxidase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 84932-52-5

References:

1. Han, M.H., Seong, B.-L., Son, H.-J. and Mheen, T.-I. Rifamycin B oxidase from Monocillium spp., a new type of diphenol oxidase. FEBS Lett. 151 (1983) 36-40. [PMID: 6825839]

[EC 1.10.3.6 created 1986]

[EC 1.10.3.7 Transferred entry: now EC 1.21.3.4, sulochrin oxidase [(+)-bisdechlorogeodin-forming] (EC 1.10.3.7 created 1986, deleted 2002)]

[EC 1.10.3.8 Transferred entry: now EC 1.21.3.5, sulochrin oxidase [(–)-bisdechlorogeodin-forming] (EC 1.10.3.8 created 1986, deleted 2002)]

EC 1.10.3.9

Accepted name: photosystem II

Reaction: 2 H2O + 2 plastoquinone + 4 = O2 + 2 plastoquinol

Systematic name: H2O:plastoquinone reductase (light-dependent)

Comments: Contains chlorophyll a, β-carotene, pheophytin, plastoquinone, a Mn4Ca cluster, heme and non-heme iron. Four successive photoreactions, resulting in a storage of four positive charges, are required to oxidize two water molecules to one oxygen molecule.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Knaff, D.B., Malkin, R., Myron, J.C. and Stoller, M. The role of plastoquinone and β-carotene in the primary reaction of plant photosystem II. Biochim. Biophys. Acta 459 (1977) 402-411. [PMID: 849432]

2. Guskov, A., Kern, J., Gabdulkhakov, A., Broser, M., Zouni, A. and Saenger, W. Cyanobacterial photosystem II at 2.9-Å resolution and the role of quinones, lipids, channels and chloride. Nat. Struct. Mol. Biol. 16 (2009) 334-342. [PMID: 19219048]

[EC 1.10.3.9 created 2011]

EC 1.10.3.10

Accepted name: ubiquinol oxidase (H+-transporting)

Reaction: 2 ubiquinol + O2 + n H+[side 1] = 2 ubiquinone + 2 H2O + n H+[side 2]

Other name(s): cytochrome bb3 oxidase; cytochrome bo-oxidase; cytochrome bd-II oxidase; ubiquinol:O2 oxidoreductase (H+-transporting)

Systematic name: ubiquinol:oxygen oxidoreductase (H+-transporting)

Comments: Contains a dinuclear centre comprising two hemes, or heme and copper. This terminal oxidase enzyme generates proton motive force by two mechanisms: (1) transmembrane charge separation resulting from utilizing protons and electrons originating from opposite sides of the membrane to generate water, and (2) active pumping of protons across the membrane. The bioenergetic efficiency (the number of charges driven across the membrane per electron used to reduce oxygen to water) depends on the enzyme; for example, for the bo3 oxidase it is 2, while for the bd-II oxidase it is 1. cf. EC 1.10.3.14, ubiquinol oxidase (electrogenic, non H+-transporting).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Abramson, J., Riistama, S., Larsson, G., Jasaitis, A., Svensson-Ek, M., Laakkonen, L., Puustinen, A., Iwata, S. and Wikstrom, M. The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. Nat. Struct. Biol. 7 (2000) 910-917. [PMID: 11017202]

2. Yap, L.L., Lin, M.T., Ouyang, H., Samoilova, R.I., Dikanov, S.A. and Gennis, R.B. The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli. Biochim. Biophys. Acta 1797 (2010) 1924-1932. [PMID: 20416270]

3. Shepherd, M., Sanguinetti, G., Cook, G.M. and Poole, R.K. Compensations for diminished terminal oxidase activity in Escherichia coli: cytochrome bd-II-mediated respiration and glutamate metabolism. J. Biol. Chem. 285 (2010) 18464-18472. [PMID: 20392690]

4. Borisov, V.B., Murali, R., Verkhovskaya, M.L., Bloch, D.A., Han, H., Gennis, R.B. and Verkhovsky, M.I. Aerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode. Proc. Natl. Acad. Sci. USA 108 (2011) 17320-17324. [PMID: 21987791]

[EC 1.10.3.10 created 2011, modified 2014]

EC 1.10.3.11

Accepted name: ubiquinol oxidase (non-electrogenic)

Reaction: 2 ubiquinol + O2 = 2 ubiquinone + 2 H2O

Other name(s): plant alternative oxidase; cyanide-insensitive oxidase; AOX (gene name); ubiquinol oxidase; ubiquinol:O2 oxidoreductase (non-electrogenic)

Systematic name: ubiquinol:oxygen oxidoreductase (non-electrogenic)

Comments: The enzyme, described from the mitochondria of plants and some fungi and protists, is an alternative terminal oxidase that is not sensitive to cyanide inhibition and does not generate a proton motive force. Unlike the electrogenic terminal oxidases that contain hemes (cf. EC 1.10.3.10 and EC 1.10.3.14), this enzyme contains a dinuclear non-heme iron complex. The function of this oxidase is believed to be dissipating excess reducing power, minimizing oxidative stress, and optimizing photosynthesis in response to changing conditions.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Bendall, D.S. and Bonner, W.D. Cyanide-insensitive respiration in plant mitochondria. Plant Physiol. 47 (1971) 236-245. [PMID: 16657603]

2. Siedow, J.N., Umbach, A.L. and Moore, A.L. The active site of the cyanide-resistant oxidase from plant mitochondria contains a binuclear iron center. FEBS Lett. 362 (1995) 10-14. [PMID: 7698344]

3. Berthold, D.A., Andersson, M.E. and Nordlund, P. New insight into the structure and function of the alternative oxidase. Biochim. Biophys. Acta 1460 (2000) 241-254. [PMID: 11106766]

4. Williams, B.A., Elliot, C., Burri, L., Kido, Y., Kita, K., Moore, A.L. and Keeling, P.J. A broad distribution of the alternative oxidase in microsporidian parasites. PLoS Pathog. 6 (2010) e1000761. [PMID: 20169184]

5. Gandin, A., Duffes, C., Day, D.A. and Cousins, A.B. The absence of alternative oxidase AOX1A results in altered response of photosynthetic carbon assimilation to increasing CO2 in Arabidopsis thaliana. Plant Cell Physiol 53 (2012) 1627-1637. [PMID: 22848123]

[EC 1.10.3.11 created 2011, modified 2014]

EC 1.10.3.12

Accepted name: menaquinol oxidase (H+-transporting)

Reaction: 2 menaquinol + O2 = 2 menaquinone + 2 H2O

Other name(s): cytochrome aa3-600 oxidase; cytochrome bd oxidase; menaquinol:O2 oxidoreductase (H+-transporting)

Systematic name: menaquinol:oxygen oxidoreductase (H+-transporting)

Comments: Cytochrome aa3-600, one of the principal respiratory oxidases from Bacillus subtilis, is a member of the heme-copper superfamily of oxygen reductases, and is a close homologue of the cytochrome bo3 ubiquinol oxidase from Escherichia coli, but uses menaquinol instead of ubiquinol as a substrate. The enzyme also pumps protons across the membrane bilayer, generating a proton motive force.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Lauraeus, M. and Wikstrom, M. The terminal quinol oxidases of Bacillus subtilis have different energy conservation properties. J. Biol. Chem. 268 (1993) 11470-11473. [PMID: 8388393]

2. Lemma, E., Simon, J., Schagger, H. and Kroger, A. Properties of the menaquinol oxidase (Qox) and of qox deletion mutants of Bacillus subtilis. Arch. Microbiol. 163 (1995) 432-438. [PMID: 7575098]

3. Yi, S.M., Narasimhulu, K.V., Samoilova, R.I., Gennis, R.B. and Dikanov, S.A. Characterization of the semiquinone radical stabilized by the cytochrome aa3-600 menaquinol oxidase of Bacillus subtilis. J. Biol. Chem. 285 (2010) 18241-18251. [PMID: 20351111]

[EC 1.10.3.12 created 2011]

EC 1.10.3.13

Accepted name: caldariellaquinol oxidase (H+-transporting)

Reaction: 2 caldariellaquinol + O2 + n H+[side 1] = 2 caldariellaquinone + 2 H2O + n H+[side 2]

Glossary: caldariellaquinol = 6-(3,7,11,15,19,23-hexamethyltetracosyl)-5-(methylsulfanyl)-1-benzothiophene-4,7-diol

Other name(s): SoxABCD quinol oxidase; SoxABCD complex; quinol oxidase SoxABCD; SoxM supercomplex; aa3-type quinol oxidase; aa3 quinol oxidase; cytochrome aa3; terminal quinol oxidase; terminal quinol:oxygen oxidoreductase; caldariella quinol:dioxygen oxidoreductase; cytochrome aa3-type oxidase; caldariellaquinol:O2 oxidoreductase (H+-transporting)

Systematic name: caldariellaquinol:oxygen oxidoreductase (H+-transporting)

Comments: A copper-containing cytochrome. The enzyme from thermophilic archaea is part of the terminal oxidase and catalyses the reduction of O2 to water, accompanied by the extrusion of protons across the cytoplasmic membrane.

Links to other databases: BRENDA, EXPASY, KEGG Metacyc, CAS registry number:

References:

1. Gleissner, M., Kaiser, U., Antonopoulos, E. and Schafer, G. The archaeal SoxABCD complex is a proton pump in Sulfolobus acidocaldarius. J. Biol. Chem. 272 (1997) 8417-8426. [PMID: 9079667]

2. Purschke, W.G., Schmidt, C.L., Petersen, A. and Schafer, G. The terminal quinol oxidase of the hyperthermophilic archaeon Acidianus ambivalens exhibits a novel subunit structure and gene organization. J. Bacteriol. 179 (1997) 1344-1353. [PMID: 9023221]

3. Gilderson, G., Aagaard, A., Gomes, C.M., Adelroth, P., Teixeira, M. and Brzezinski, P. Kinetics of electron and proton transfer during O2 reduction in cytochrome aa3 from A. ambivalens: an enzyme lacking Glu(I-286). Biochim.Biophys. Acta 1503 (2001) 261-270. [PMID: 11115638]

4. Komorowski, L., Verheyen, W. and Schafer, G. The archaeal respiratory supercomplex SoxM from S. acidocaldarius combines features of quinole and cytochrome c oxidases. Biol. Chem. 383 (2002) 1791-1799. [PMID: 12530544]

5. Muller, F.H., Bandeiras, T.M., Urich, T., Teixeira, M., Gomes, C.M. and Kletzin, A. Coupling of the pathway of sulphur oxidation to dioxygen reduction: characterization of a novel membrane-bound thiosulphate:quinone oxidoreductase. Mol. Microbiol. 53 (2004) 1147-1160. [PMID: 15306018]

6. Bandeiras, T.M., Pereira, M.M., Teixeira, M., Moenne-Loccoz, P. and Blackburn, N.J. Structure and coordination of CuB in the Acidianus ambivalens aa3 quinol oxidase heme-copper center. J. Biol. Inorg. Chem. 10 (2005) 625-635. [PMID: 16163550]

[EC 1.10.3.13 created 2013]

EC 1.10.3.14

Accepted name: ubiquinol oxidase (electrogenic, non H+-transporting)

Reaction: 2 ubiquinol + O2 + 4 H+[side 1] = 2 ubiquinone + 2 H2O + 4 H+[side 2]

Other name(s): cytochrome bd-I oxidase; cydA (gene name); cydB (gene name); ubiquinol:O2 oxidoreductase (electrogenic, non H+-transporting)

Systematic name: ubiquinol:oxygen oxidoreductase (electrogenic, non H+-transporting)

Comments: This terminal oxidase enzyme is unable to pump protons but generates a proton motive force by transmembrane charge separation resulting from utilizing protons and electrons originating from opposite sides of the membrane to generate water. The bioenergetic efficiency (the number of charges driven across the membrane per electron used to reduce oxygen to water) is 1. The bd-I oxidase from the bacterium Escherichia coli is the predominant respiratory oxygen reductase that functions under microaerophilic conditions in that organism. cf. EC 1.10.3.10, ubiquinol oxidase (H+-transporting).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Miller, M.J., Hermodson, M. and Gennis, R.B. The active form of the cytochrome d terminal oxidase complex of Escherichia coli is a heterodimer containing one copy of each of the two subunits. J. Biol. Chem. 263 (1988) 5235-5240. [PMID: 3281937]

2. Puustinen, A., Finel, M., Haltia, T., Gennis, R.B. and Wikstrom, M. Properties of the two terminal oxidases of Escherichia coli. Biochemistry 30 (1991) 3936-3942. [PMID: 1850294]

3. Belevich, I., Borisov, V.B., Zhang, J., Yang, K., Konstantinov, A.A., Gennis, R.B. and Verkhovsky, M.I. Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site. Proc. Natl. Acad. Sci. USA 102 (2005) 3657-3662. [PMID: 15728392]

4. Lenn, T., Leake, M.C. and Mullineaux, C.W. Clustering and dynamics of cytochrome bd-I complexes in the Escherichia coli plasma membrane in vivo. Mol. Microbiol. 70 (2008) 1397-1407. [PMID: 19019148]

[EC 1.10.3.14 created 2014]

EC 1.10.3.15

Accepted name: grixazone synthase

Reaction: 2 3-amino-4-hydroxybenzoate + N-acetyl-L-cysteine + 2 O2 = grixazone B + 4 H2O + CO2

For diagram of reaction click here.

Glossary: grixazone B = 8-amino-9-(N-acetyl-L-cystein-S-yl)-7-oxo-7H-phenoxazine-2-carboxylic acid

Other name(s): GriF

Systematic name: 3-amino-4-hydroxybenzoate:N-acetyl-L-cysteine:oxygen oxidoreductase

Comments: A type 3 multi copper protein. The enzyme, isolated from the bacterium Streptomyces griseus, catalyses an 8 electron oxidation. Activation of the enzyme requires a copper chaperone (GriE). It also acts on 3-amino-4-hydroxybenzaldehyde, giving grixazone A. The second aldehyde group is presumably lost as formate. The enzyme also catalyses the reaction of EC 1.10.3.4 o-aminophenol oxidase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Suzuki, H., Ohnishi, Y., Furusho, Y., Sakuda, S. and Horinouchi, S. Novel benzene ring biosynthesis from C3 and C4 primary metabolites by two enzymes. J. Biol. Chem. 281 (2006) 36944-36951. [PMID: 17003031]

2. Le Roes-Hill, M., Goodwin, C. and Burton, S. Phenoxazinone synthase: what’s in a name. Trends Biotechnol 27 (2009) 248-258. [PMID: 19268377]

[EC 1.10.3.15 created 2014]

EC 1.10.3.16

Accepted name: dihydrophenazinedicarboxylate synthase

Reaction: (1) (1R,6R)-1,4,5,5a,6,9-hexahydrophenazine-1,6-dicarboxylate + O2 = (1R,10aS)-1,4,10,10a-tetrahydrophenazine-1,6-dicarboxylate + H2O2
(2) (1R,10aS)-1,4,10,10a-tetrahydrophenazine-1,6-dicarboxylate + O2 = (5aS)-5,5a-dihydrophenazine-1,6-dicarboxylate + H2O2
(3) (1R,10aS)-1,4,10,10a-tetrahydrophenazine-1-carboxylate + O2 = (10aS)-10,10a-dihydrophenazine-1-carboxylate + H2O2
(4) (1R)-1,4,5,10-tetrahydrophenazine-1-carboxylate + O2 = (10aS)-5,10-dihydrophenazine-1-carboxylate + H2O2

Other name(s): phzG (gene name)

Systematic name: 1,4,5a,6,9,10a-hexahydrophenazine-1,6-dicarboxylate:oxygen oxidoreductase

Comments: Requires FMN. The enzyme, isolated from the bacteria Pseudomonas fluorescens 2-79 and Burkholderia lata 383, is involved in biosynthesis of the reduced forms of phenazine, phenazine-1-carboxylate, and phenazine-1,6-dicarboxylate, where it catalyses multiple reactions.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Xu, N., Ahuja, E.G., Janning, P., Mavrodi, D.V., Thomashow, L.S. and Blankenfeldt, W. Trapped intermediates in crystals of the FMN-dependent oxidase PhzG provide insight into the final steps of phenazine biosynthesis. Acta Crystallogr. D Biol. Crystallogr. 69 (2013) 1403-1413. [PMID: 23897464]

[EC 1.10.3.16 created 2016]


EC 1.10.5 With a quinone or related compound as acceptor

EC 1.10.5.1

Accepted name: ribosyldihydronicotinamide dehydrogenase (quinone)

Reaction: 1-(β-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone = 1-(β-D-ribofuranosyl)nicotinamide + a quinol

For diagram of reaction click here.

Other name(s): NRH:quinone oxidoreductase 2; NQO2; NAD(P)H:quinone oxidoreductase-2 (misleading); QR2; quinone reductase 2; N-ribosyldihydronicotinamide dehydrogenase (quinone); NAD(P)H:quinone oxidoreductase2 (misleading)

Systematic name: 1-(β-D-ribofuranosyl)-1,4-dihydronicotinamide:quinone oxidoreductase

Comments: A flavoprotein. Unlike EC 1.6.5.2, NAD(P)H dehydrogenase (quinone), this quinone reductase cannot use NADH or NADPH; instead it uses N-ribosyl- and N-alkyldihydronicotinamides. Polycyclic aromatic hydrocarbons, such as benz[a]anthracene, and the estrogens 17β-estradiol and diethylstilbestrol are potent inhibitors, but dicoumarol is only a very weak inhibitor [2]. This enzyme can catalyse both 2-electron and 4-electron reductions, but one-electron acceptors, such as potassium ferricyanide, cannot be reduced [3].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Liao, S., Dulaney, J.T. and Williams-Ashman, H.G. Purification and properties of a flavoprotein catalyzing the oxidation of reduced ribosyl nicotinamide. J. Biol. Chem. 237 (1962) 2981-2987. [PMID: 14465018]

2. Zhao, Q., Yang, X.L., Holtzclaw, W.D. and Talalay, P. Unexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase). Proc. Natl. Acad. Sci. USA 94 (1997) 1669-1674. [PMID: 9050836]

3. Wu, K., Knox, R., Sun, X.Z., Joseph, P., Jaiswal, A.K., Zhang, D., Deng, P.S. and Chen, S. Catalytic properties of NAD(P)H:quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase. Arch. Biochem. Biophys. 347 (1997) 221-228. [PMID: 9367528]

4. Jaiswal, A.K. Human NAD(P)H:quinone oxidoreductase2. Gene structure, activity, and tissue-specific expression. J. Biol. Chem. 269 (1994) 14502-14508. [PMID: 8182056]

[EC 1.10.5.1 created 2005 as EC 1.10.99.2, transfered 2015 to EC 1.10.5.1]


EC 1.10.9 With a copper protein as acceptor

EC 1.10.9.1

Accepted name: plastoquinol—plastocyanin reductase

Reaction: plastoquinol + 2 oxidized plastocyanin + 2 H+[side 1] = plastoquinone + 2 reduced plastocyanin + 4 H+[side 2]

Other name(s): plastoquinol/plastocyanin oxidoreductase; cytochrome b6/f complex; cytochrome b6/ complex

Systematic name: plastoquinol:oxidized-plastocyanin oxidoreductase

Comments: Contains two b-type cytochromes, two c-type cytochromes (cn and f), and a [2Fe-2S] Rieske cluster. The enzyme plays a key role in photosynthesis, transferring electrons from photosystem II (EC 1.10.3.9) to photosystem I (EC 1.97.1.12). Cytochrome c-552 can act as acceptor instead of plastocyanin, but more slowly. In chloroplasts, protons are translocated through the thylakoid membrane from the stroma to the lumen. The mechanism occurs through the Q cycle as in EC 1.10.2.2, quinol—cytochrome-c reductase (complex III) and involves electron bifurcation.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 79079-13-3

References:

1. Hurt, E. and Hauska, G. A cytochrome f/b6 complex of five polypeptides with plastoquinol-plastocyanin-oxidoreductase activity from spinach chloroplasts. Eur. J. Biochem. 117 (1981) 591-595. [PMID: 6269845]

2. Cramer, W.A. and Zhang, H. Consequences of the structure of the cytochrome b6f complex for its charge transfer pathways. Biochim. Biophys. Acta 1757 (2006) 339-345. [PMID: 16787635]

[EC 1.10.9.1 created 1984 as EC 1.10.99.1, transferred 2011 to EC 1.10.9.1]


EC 1.10.99 With unknown physiological acceptors

Contents

EC 1.10.99.1 now EC 1.10.9.1
EC 1.10.99.2 now EC 1.10.5.1
EC 1.10.99.3 now EC 1.23.5.1

[EC 1.10.99.1 Transferred entry: Now EC 1.10.9.1 plastoquinol—plastocyanin reductase (EC 1.10.99.1 created 1984, deleted 2011)]

[EC 1.10.99.2 Transferred entry: ribosyldihydronicotinamide dehydrogenase (quinone). Now classified as EC 1.10.5.1, ribosyldihydronicotinamide dehydrogenase (quinone). (EC 1.10.99.2 created 2005, deleted 2014)]

[EC 1.10.99.3 Transferred entry: violaxanthin de-epoxidase. Now classified as EC 1.23.5.1, violaxanthin de-epoxidase. (EC 1.10.99.3 created 2005, deleted 2014)]


EC 1.11 ACTING ON PEROXIDE AS DONORS

Sections

EC 1.11.1 Peroxidases
EC 1.11.2 With H2O2 as acceptor, one oxygen atom of which is incorporated into the product


EC 1.11.1 Peroxidases

Contents

EC 1.11.1.1 NADH peroxidase
EC 1.11.1.2 NADPH peroxidase
EC 1.11.1.3 fatty-acid peroxidase
EC 1.11.1.4 now EC 1.13.11.11
EC 1.11.1.5 cytochrome-c peroxidase
EC 1.11.1.6 catalase
EC 1.11.1.7 peroxidase
EC 1.11.1.8 iodide peroxidase
EC 1.11.1.9 glutathione peroxidase
EC 1.11.1.10 chloride peroxidase
EC 1.11.1.11 L-ascorbate peroxidase
EC 1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase
EC 1.11.1.13 manganese peroxidase
EC 1.11.1.14 lignin peroxidase
EC 1.11.1.15 peroxiredoxin
EC 1.11.1.16 versatile peroxidase
EC 1.11.1.17 glutathione amide-dependent peroxidase
EC 1.11.1.18 bromide peroxidase
EC 1.11.1.19 dye decolorizing peroxidase
EC 1.11.1.20 prostamide/prostaglandin F synthase
EC 1.11.1.21 catalase-peroxidase
EC 1.11.1.22 hydroperoxy fatty acid reductase
EC 1.11.1.23 (S)-2-hydroxypropylphosphonic acid epoxidase

EC 1.11.1.1

Accepted name: NADH peroxidase

Reaction: NADH + H+ + H2O2 = NAD+ + 2 H2O

Other name(s): DPNH peroxidase; NAD peroxidase; diphosphopyridine nucleotide peroxidase; NADH-peroxidase; nicotinamide adenine dinucleotide peroxidase; NADH2 peroxidase

Systematic name: NADH:hydrogen-peroxide oxidoreductase

Comments: A flavoprotein (FAD). Ferricyanide, quinones, etc., can replace H2O2.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9032-24-0

References:

1. Domagk, G.F. and Horecker, B.L. Fructose and erythrose metabolism in Alcaligenes faecalis. Arch. Biochem. Biophys. 109 (1965) 342-349.

2. Mizushima, S. and Kitahara, K. Purification and properties of DPNH peroxidase in Lactobacillus casei. J. Gen. Appl. Microbiol. 8 (1962) 56-62.

3. Walker, G.A. and Kilgour, G.L. Pyridine nucleotide oxidizing enzymes of Lactobacillus casei. II. Oxidase and peroxidase. Arch. Biochem. Biophys. 131 (1965) 534-539. [PMID: 4285876]

[EC 1.11.1.1 created 1961]

EC 1.11.1.2

Accepted name: NADPH peroxidase

Reaction: NADPH + H+ + H2O2 = NADP+ + 2 H2O

Other name(s): TPNH peroxidase; NADP peroxidase; nicotinamide adenine dinucleotide phosphate peroxidase; TPN peroxidase; triphosphopyridine nucleotide peroxidase; NADPH2 peroxidase

Systematic name: NADPH:hydrogen-peroxide oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9029-51-0

References:

1. Conn, E.E., Kraemer, L.M., Liu, P.N. and Vennesland, B. The aerobic oxidation of reduced triphosphopyridine nucleotide by a wheat germ enzyme system. J. Biol. Chem. 194 (1952) 143-151.

[EC 1.11.1.2 created 1961]

EC 1.11.1.3

Accepted name: fatty-acid peroxidase

Reaction: palmitate + 2 H2O2 = pentadecanal + CO2 + 3 H2O

Other name(s): long chain fatty acid peroxidase

Systematic name: hexadecanoate:hydrogen-peroxide oxidoreductase

Comments: Acts on long-chain fatty acids from dodecanoic to octadecanoic acid.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9029-52-1

References:

1. Martin, R.O. and Stumpf, P.K. Fat metabolism in higher plants. XII. α-Oxidation of long chain fatty acids. J. Biol. Chem. 234 (1959) 2548-2554.

[EC 1.11.1.3 created 1961]

[EC 1.11.1.4 Transferred entry: now EC 1.13.11.11 tryptophan 2,3-dioxygenase (EC 1.11.1.4 created 1961, deleted 1964, reinstated 1965 as EC 1.13.1.12, deleted 1972)]

EC 1.11.1.5

Accepted name: cytochrome-c peroxidase

Reaction: 2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O

Other name(s): cytochrome peroxidase; cytochrome c-551 peroxidase; apocytochrome c peroxidase; mesocytochrome c peroxidase azide; mesocytochrome c peroxidase cyanide; mesocytochrome c peroxidase cyanate; cytochrome c-H2O oxidoreductase; cytochrome c peroxidase

Systematic name: ferrocytochrome-c:hydrogen-peroxide oxidoreductase

Comments: A hemoprotein.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-53-2

References:

1. Altschul, A.M., Abrams, R. and Hogness, T.R. Cytochrome c peroxidase. J. Biol. Chem. 136 (1940) 777-794.

2. Yamanaka, T. and Okunuki, K. Isolation of a cytochrome peroxidase from Thiobacillus novellus. Biochim. Biophys. Acta 220 (1970) 354-356. [PMID: 5487887]

3. Yonetani, T. Cytochrome c peroxidase. Adv. Enzymol. Relat. Areas Mol. Biol. 33 (1970) 309-335. [PMID: 4318313]

[EC 1.11.1.5 created 1961]

EC 1.11.1.6

Accepted name: catalase

Reaction: 2 H2O2 = O2 + 2 H2O

Other name(s): equilase; caperase; optidase; catalase-peroxidase; CAT

Systematic name: hydrogen-peroxide:hydrogen-peroxide oxidoreductase

Comments: A hemoprotein. A manganese protein containing MnIII in the resting state, which also belongs here, is often called pseudocatalase. The enzymes from some organisms, such as Penicillium simplicissimum, can also act as a peroxidase (EC 1.11.1.7) for which several organic substances, especially ethanol, can act as a hydrogen donor. Enzymes that exhibit both catalase and peroxidase activity belong under EC 1.11.1.21, catalase-peroxidase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9001-05-2

References:

1. Herbert, D. and Pinsent, J. Crystalline bacterial catalase. Biochem. J. 43 (1948) 193-202. [PMID: 16748386]

2. Herbert, D. and Pinsent, J. Crystalline human erythrocyte catalase. Biochem. J. 43 (1948) 203-205. [PMID: 16748387]

3. Keilin, D. and Hartree, E.F. Coupled oxidation of alcohol. Proc. R. Soc. Lond. B Biol. Sci. 119 (1936) 141-159.

4. Kono, Y. and Fridovich, I. Isolation and characterization of the pseudocatalase of Lactobacillus plantarum. J. Biol. Chem. 258 (1983) 6015-6019. [PMID: 6853475]

5. Nicholls, P. and Schonbaum, G.R. Catalases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 147-225.

[EC 1.11.1.6 created 1961, modified 1986, modified 1999, modified 2013]

EC 1.11.1.7

Accepted name: peroxidase

Reaction: 2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O

Other name(s): lactoperoxidase; guaiacol peroxidase; plant peroxidase; Japanese radish peroxidase; horseradish peroxidase (HRP); soybean peroxidase (SBP); extensin peroxidase; heme peroxidase; oxyperoxidase; protoheme peroxidase; pyrocatechol peroxidase; scopoletin peroxidase, Coprinus cinereus peroxidase, Arthromyces ramosus peroxidase

Systematic name: phenolic donor:hydrogen-peroxide oxidoreductase

Comments: Heme proteins with histidine as proximal ligand. The iron in the resting enzyme is Fe(III). They also peroxidize non-phenolic substrates such as 3,3',5,5'-tetramethylbenzidine (TMB) and 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS). Certain peroxidases (e.g. lactoperoxidase, SBP) oxidize bromide, iodide and thiocyanate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9003-99-0

References:

1. Kenten, R.H. and Mann, P.J.G. Simple method for the preparation of horseradish peroxidase. Biochem. J. 57 (1954) 347-348. [PMID: 13172193]

2. Morrison, M., Hamilton, H.B. and Stotz, E. The isolation and purification of lactoperoxidase by ion exchange chromatography. J. Biol. Chem. 228 (1957) 767-776. [PMID: 13475358]

3. Paul, K.G. Peroxidases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 227-274.

4. Tagawa, K., Shin, M. and Okunuki, K. Peroxidases from wheat germ. Nature (Lond.) 183 (1959) 111. [PMID: 13622706]

5. Theorell, H. The preparation and some properties of crystalline horse-radish peroxidase. Ark. Kemi Mineral. Geol. 16A No. 2 (1943) 1-11.

6. Farhangrazi, Z.S., Copeland, B.R., Nakayama, T., Amachi, T., Yamazaki, I. and Powers, L.S. Oxidation-reduction properties of compounds I and II of Arthromyces ramosus peroxidase. Biochemistry 33 (1994) 5647-5652. [PMID: 8180190]

7. Aitken, M.D. and Heck, P.E. Turnover capacity of coprinus cinereus peroxidase for phenol and monosubstituted phenol. Biotechnol. Prog. 14 (1998) 487-492. [PMID: 9622531]

8. Dunford, H.B. Heme peroxidases, Wiley-VCH, New York, 1999, pp. 33-218.

9. Torres, E and Ayala, M. Biocatalysis based on heme peroxidases, Springer, Berlin, 2010, pp. 7-110.

[EC 1.11.1.7 created 1961, modified 2010, modified 2011]

EC 1.11.1.8

Accepted name: iodide peroxidase

Reaction: (1) 2 iodide + H2O2 + 2 H+ = diiodine + 2 H2O
(2) [thyroglobulin]-L-tyrosine + iodide + H2O2 = [thyroglobulin]-3-iodo-L-tyrosine + 2 H2O
(3) [thyroglobulin]-3-iodo-L-tyrosine + iodide + H2O2 = [thyroglobulin]-3,5-diiodo-L-tyrosine + 2 H2O
(4) 2 [thyroglobulin]-3,5-diiodo-L-tyrosine + H2O2 = [thyroglobulin]-L-thyroxine + [thyroglobulin]-aminoacrylate + 2 H2O
(5) [thyroglobulin]-3-iodo-L-tyrosine + [thyroglobulin]-3,5-diiodo-L-tyrosine + H2O2 = [thyroglobulin]-3,5,3'-triiodo-L-thyronine + [thyroglobulin]-aminoacrylate + 2 H2O

Glossary: 3,5,3'-triiodo-L-thyronine = triiodo-L-thyronine

Other name(s): thyroid peroxidase; iodotyrosine deiodase; iodinase; iodoperoxidase (heme type); iodide peroxidase-tyrosine iodinase; iodotyrosine deiodinase; monoiodotyrosine deiodinase; thyroperoxidase; tyrosine iodinase; TPO

Systematic name: iodide:hydrogen-peroxide oxidoreductase

Comments: Thyroid peroxidase catalyses the biosynthesis of the thyroid hormones L-thyroxine and triiodo-L-thyronine. It catalyses both the iodination of tyrosine residues in thyroglobulin (forming mono- and di-iodinated forms) and their coupling to form either L-thyroxine or triiodo-L-thyronine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9031-28-1

References:

1. Cunningham, B.A. and Kirkwood, S. Enzyme systems concerned with the synthesis of monoiodotyrosine. III. Ion requirements of the soluble system. J. Biol. Chem. 236 (1961) 485-489. [PMID: 13718859]

2. Hosoya, T., Kondo, Y. and Ui, N. Peroxidase activity in thyroid gland and partial purification of the enzyme. J. Biochem. (Tokyo) 52 (1962) 180-189. [PMID: 13964156]

3. Coval, M.L. and Taurog, A. Purification and iodinating activity of hog thyroid peroxidase. J. Biol. Chem. 242 (1967) 5510-5523. [PMID: 12325367]

4. Gavaret, J.M., Cahnmann, H.J. and Nunez, J. Thyroid hormone synthesis in thyroglobulin. The mechanism of the coupling reaction. J. Biol. Chem. 256 (1981) 9167-9173. [PMID: 7021557]

5. Ohtaki, S., Nakagawa, H., Nakamura, M. and Yamazaki, I. One- and two-electron oxidations of tyrosine, monoiodotyrosine, and diiodotyrosine catalyzed by hog thyroid peroxidase. J. Biol. Chem. 257 (1982) 13398-13403. [PMID: 7142155]

6. Magnusson, R.P., Taurog, A. and Dorris, M.L. Mechanism of iodide-dependent catalatic activity of thyroid peroxidase and lactoperoxidase. J. Biol. Chem. 259 (1984) 197-205. [PMID: 6706930]

7. Virion, A., Courtin, F., Deme, D., Michot, J.L., Kaniewski, J. and Pommier, J. Spectral characteristics and catalytic properties of thyroid peroxidase-H2O2 compounds in the iodination and coupling reactions. Arch. Biochem. Biophys. 242 (1985) 41-47. [PMID: 2996435]

8. Rawitch, A.B., Pollock, G., Yang, S.X. and Taurog, A. Thyroid peroxidase glycosylation: the location and nature of the N-linked oligosaccharide units in porcine thyroid peroxidase. Arch. Biochem. Biophys. 297 (1992) 321-327. [PMID: 1497352]

9. Sun, W. and Dunford, H.B. Kinetics and mechanism of the peroxidase-catalyzed iodination of tyrosine. Biochemistry 32 (1993) 1324-1331. [PMID: 8448141]

10. Taurog, A., Dorris, M.L. and Doerge, D.R. Mechanism of simultaneous iodination and coupling catalyzed by thyroid peroxidase. Arch. Biochem. Biophys. 330 (1996) 24-32. [PMID: 8651700]

11. Ruf, J. and Carayon, P. Structural and functional aspects of thyroid peroxidase. Arch. Biochem. Biophys. 445 (2006) 269-277. [PMID: 16098474]

[EC 1.11.1.8 created 1961, modified 2012]

EC 1.11.1.9

Accepted name: glutathione peroxidase

Reaction: 2 glutathione + H2O2 = glutathione disulfide + 2 H2O

Other name(s): GSH peroxidase; selenium-glutathione peroxidase; reduced glutathione peroxidase

Systematic name: glutathione:hydrogen-peroxide oxidoreductase

Comments: A protein containing a selenocysteine residue. Steroid and lipid hydroperoxides, but not the product of reaction of EC 1.13.11.12 lipoxygenase on phospholipids, can act as acceptor, but more slowly than H2O2 (cf. EC 1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9013-66-5

References:

1. Chaudiere, J. and Tappel, A.L. Purification and characterization of selenium-glutathione peroxidase from hamster liver. Arch. Biochem. Biophys. 226 (1983) 448-457. [PMID: 6227287]

2. Grossmann, A. and Wendel, A. Non-reactivity of the selenoenzyme glutathione peroxidase with enzymatically hydroperoxidized phospholipids. Eur. J. Biochem. 135 (1983) 549-552. [PMID: 6413205]

3. Nakamura, W., Hosoda, S. and Hayashi, K. Purification and properties of rat liver glutathione peroxidase. Biochim. Biophys. Acta 358 (1974) 251-261.

[EC 1.11.1.9 created 1965, modified 1989]

EC 1.11.1.10

Accepted name: chloride peroxidase

Reaction: RH + chloride + H2O2 = RCl + 2 H2O

Other name(s): chloroperoxidase; CPO; vanadium haloperoxidase

Systematic name: chloride:hydrogen-peroxide oxidoreductase

Comments: Brings about the chlorination of a range of organic molecules, forming stable C-Cl bonds. Also oxidizes bromide and iodide. Enzymes of this type are either heme-thiolate proteins, or contain vanadate. A secreted enzyme produced by the ascomycetous fungus Caldariomyces fumago (Leptoxyphium fumago) is an example of the heme-thiolate type. It catalyses the production of hypochlorous acid by transferring one oxygen atom from H2O2 to chloride. At a separate site it catalyses the chlorination of activated aliphatic and aromatic substrates, via HClO and derived chlorine species. In the absence of halides, it shows peroxidase (e.g. phenol oxidation) and peroxygenase activities. The latter inserts oxygen from H2O2 into, for example, styrene (side chain epoxidation) and toluene (benzylic hydroxylation), however, these activities are less pronounced than its activity with halides. Has little activity with non-activated substrates such as aromatic rings, ethers or saturated alkanes. The chlorinating peroxidase produced by ascomycetous fungi (e.g. Curvularia inaequalis) is an example of a vanadium chloroperoxidase, and is related to bromide peroxidase (EC 1.11.1.18). It contains vanadate and oxidizes chloride, bromide and iodide into hypohalous acids. In the absence of halides, it peroxygenates organic sulfides and oxidizes ABTS [2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)] but no phenols.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9055-20-3

References:

1. Morris, D.R. and Hager, L.P. Chloroperoxidase. I. Isolation and properties of the crystalline glycoprotein. J. Biol. Chem. 241 (1966) 1763-1768. [PMID: 5949836]

2. Hager, L.P., Hollenberg, P.F., Rand-Meir, T., Chiang, R. and Doubek, D.L. Chemistry of peroxidase intermediates. Ann. N.Y. Acad. Sci. 244 (1975) 80-93. [PMID: 1056179]

3. Theiler, R., Cook, J.C., Hager, L.P. and Siuda, J.F. Halohydrocarbon synthesis by bromoperoxidase. Science 202 (1978) 1094-1096. [PMID: 17777960]

4. Sundaramoorthy, M., Terner, J. and Poulos, T.L. The crystal structure of chloroperoxidase: a heme peroxidase—cytochrome P450 functional hybrid. Structure 3 (1995) 1367-1377. [PMID: 8747463]

5. ten Brink, H.B., Tuynman, A., Dekker, H.L., Hemrika, W., Izumi, Y., Oshiro, T., Schoemaker, H.E. and Wever, R. Enantioselective sulfoxidation catalyzed by vanadium haloperoxidases. Inorg. Chem. 37 (1998) 6780-6784. [PMID: 11670813]

6. ten Brink, H.B., Dekker, H.L., Schoemaker, H.E. and Wever, R. Oxidation reactions catalyzed by vanadium chloroperoxidase from Curvularia inaequalis. J. Inorg. Biochem. 80 (2000) 91-98. [PMID: 10885468]

7. Manoj, K.M. Chlorinations catalyzed by chloroperoxidase occur via diffusible intermediate(s) and the reaction components play multiple roles in the overall process. Biochim. Biophys. Acta 1764 (2006) 1325-1339. [PMID: 16870515]

8. Kuhnel, K., Blankenfeldt, W., Terner, J. and Schlichting, I. Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate. J. Biol. Chem. 281 (2006) 23990-23998. [PMID: 16790441]

9. Manoj, K.M. and Hager, L.P. Chloroperoxidase, a janus enzyme. Biochemistry 47 (2008) 2997-3003. [PMID: 18220360]

[EC 1.11.1.10 created 1972, modified 2011]

EC 1.11.1.11

Accepted name: L-ascorbate peroxidase

Reaction: 2 L-ascorbate + H2O2 + 2 H+ = L-ascorbate + L-dehydroascorbate + 2 H2O (overall reaction)
(1a) 2 L-ascorbate + H2O2 + 2 H+ = 2 monodehydroascorbate + 2 H2O
(1b) 2 monodehydroascorbate = L-ascorbate + L-dehydroascorbate (spontaneous)

Glossary: monodehydroascorbate = ascorbate radical

Other name(s): L-ascorbic acid peroxidase; L-ascorbic acid-specific peroxidase; ascorbate peroxidase; ascorbic acid peroxidase

Systematic name: L-ascorbate:hydrogen-peroxide oxidoreductase

Comments: A heme protein. Oxidizes ascorbate and low molecular weight aromatic substrates. The monodehydroascorbate radical produced is either directly reduced back to ascorbate by EC 1.6.5.4 [monodehydroascorbate reductase (NADH)] or undergoes non-enzymatic disproportionation to ascorbate and dehydroascorbate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 72906-87-7

References:

1. Shigeoka, S., Nakano, Y. and Kitaoka, S. Purification and some properties of L-ascorbic-acid-specific peroxidase in Euglena gracilis. Z. Arch. Biochem. Biophys. 201 (1980) 121-127. [PMID: 6772104]

2. Shigeoka, S., Nakano, Y. and Kitaoka, S. Metabolism of hydrogen peroxide in Euglena gracilis Z by L-ascorbic acid peroxidase. Biochem. J. 186 (1980) 377-380. [PMID: 6768357]

3. Nakano, Y and Asada, K. Purification of ascorbate peroxidase in spinach chloroplasts; its inactivation in ascorbate-depleted medium and reactivation by monodehydroascorbate radical. Plant Cell Physiol. 28 (1987) 131-140.

4. Patterson, W.R. and Poulos, T.L. Crystal structure of recombinant pea cytosolic ascorbate peroxidase. Biochemistry 34 (1995) 4331-4341. [PMID: 7703247]

5. Sharp, K.H., Moody, P.C., Brown, K.A. and Raven, E.L. Crystal structure of the ascorbate peroxidase-salicylhydroxamic acid complex. Biochemistry 43 (2004) 8644-8651. [PMID: 15236572]

6. Macdonald, I.K., Badyal, S.K., Ghamsari, L., Moody, P.C. and Raven, E.L. Interaction of ascorbate peroxidase with substrates: a mechanistic and structural analysis. Biochemistry 45 (2006) 7808-7817. [PMID: 16784232]

[EC 1.11.1.11 created 1983, modified 2010, modified 2011]

EC 1.11.1.12

Accepted name: phospholipid-hydroperoxide glutathione peroxidase

Reaction: 2 glutathione + a hydroperoxy-fatty-acyl-[lipid] = glutathione disulfide + a hydroxy-fatty-acyl-[lipid] + H2O

Other name(s): peroxidation-inhibiting protein; PHGPX; peroxidation-inhibiting protein:peroxidase,glutathione (phospholipid hydroperoxide-reducing); phospholipid hydroperoxide glutathione peroxidase; hydroperoxide glutathione peroxidase

Systematic name: glutathione:lipid-hydroperoxide oxidoreductase

Comments: A protein containing a selenocysteine residue. The products of action of EC 1.13.11.12 lipoxygenase on phospholipids can act as acceptors; H2O2 can also act, but much more slowly (cf. EC 1.11.1.9 glutathione peroxidase).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 97089-70-8

References:

1. Ursini, F., Maiorino, M. and Gregolin, C. The selenoenzyme phospholipid hydroperoxide glutathione peroxidase. Biochim. Biophys. Acta 839 (1985) 62-70. [PMID: 3978121]

2. Schnurr, K., Belkner, J., Ursini, F., Schewe, T. and Kuhn, H. The selenoenzyme phospholipid hydroperoxide glutathione peroxidase controls the activity of the 15-lipoxygenase with complex substrates and preserves the specificity of the oxygenation products. J. Biol. Chem. 271 (1996) 4653-4658. [PMID: 8617728]

[EC 1.11.1.12 created 1989, modified 2015]

EC 1.11.1.13

Accepted name: manganese peroxidase

Reaction: 2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O

Other name(s): peroxidase-M2; Mn-dependent (NADH-oxidizing) peroxidase

Systematic name: Mn(II):hydrogen-peroxide oxidoreductase

Comments: A hemoprotein. The enzyme from white rot basidiomycetes is involved in the oxidative degradation of lignin. The enzyme oxidizes a bound Mn2+ ion to Mn3+ in the presence of hydrogen peroxide. The product, Mn3+, is released from the active site in the presence of a chelator (mostly oxalate and malate) that stabilizes it against disproportionation to Mn2+ and insoluble Mn4+ [4]. The complexed Mn3+ ion can diffuse into the lignified cell wall, where it oxidizes phenolic components of lignin and other organic substrates [1]. It is inactive with veratryl alcohol or nonphenolic substrates.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 114995-15-2

References:

1. Glenn, J.K., Akileswaran, L. and Gold, M.H. Mn(II) oxidation is the principal function of the extracellular Mn-peroxidase from Phanerochaete chrysosporium. Arch. Biochem. Biophys. 251 (1986) 688-696.

2. Paszczynski, A., Huynh, V.-B. and Crawford, R. Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium. Arch. Biochem. Biophys. 244 (1986) 750-765. [PMID: 3080953]

3. Wariishi, H., Akileswaran, L. and Gold, M.H. Manganese peroxidase from the basidiomycete Phanerochaete chrysosporium: spectral characterization of the oxidized states and the catalytic cycle. Biochemistry 27 (1988) 5365-5370.

4. Kuan, I.C. and Tien, M. Stimulation of Mn peroxidase activity: a possible role for oxalate in lignin biodegradation. Proc. Natl. Acad. Sci. USA 90 (1993) 1242-1246. [PMID: 8433984]

[EC 1.11.1.13 created 1992]

EC 1.11.1.14

Accepted name: lignin peroxidase

Reaction: (1) 1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O
(2) 2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O

Glossary: veratryl alcohol = (3,4-dimethoxyphenyl)methanol
veratraldehyde = 3,4-dimethoxybenzaldehyde
2-methoxyphenol = guaiacol

Other name(s): diarylpropane oxygenase; ligninase I; diarylpropane peroxidase; LiP; diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving); 1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol:hydrogen-peroxide oxidoreductase (incorrect); (3,4-dimethoxyphenyl)methanol:hydrogen-peroxide oxidoreductase

Systematic name: 1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol:hydrogen-peroxide oxidoreductase

Comments: A hemoprotein, involved in the oxidative breakdown of lignin by white-rot basidiomycete fungi. The reaction involves an initial oxidation of the heme iron by hydrogen peroxide, forming compound I (FeIV=O radical cation) at the active site. A single one-electron reduction of compound I by an electron derived from a substrate molecule yields compound II (FeIV=O non-radical cation), followed by a second one-electron transfer that returns the enzyme to the ferric oxidation state. The electron transfer events convert the substrate molecule into a transient cation radical intermediate that fragments spontaneously. The enzyme can act on a wide range of aromatic compounds, including methoxybenzenes and nonphenolic β-O-4 linked arylglycerol β-aryl ethers, but cannot act directly on the lignin molecule, which is too large to fit into the active site. However larger lignin molecules can be degraded in the presence of veratryl alcohol. It has been suggested that the free radical that is formed when the enzyme acts on veratryl alcohol can diffuse into the lignified cell wall, where it oxidizes lignin and other organic substrates. In the presence of high concentration of hydrogen peroxide and lack of substrate, the enzyme forms a catalytically inactive form (compound III). This form can be rescued by interaction with two molecules of the free radical products. In the case of veratryl alcohol, such an interaction yields two molecules of veratryl aldehyde.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 93792-13-3

References:

1. Kersten, P.J., Tien, M., Kalyanaraman, B. and Kirk, T.K. The ligninase of Phanerochaete chrysosporium generates cation radicals from methoxybenzenes. J. Biol. Chem. 260 (1985) 2609-2612. [PMID: 2982828]

2. Paszczynski, A., Huynh, V.-B. and Crawford, R. Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium, Arch. Biochem. Biophys. 244 (1986) 750-765. [PMID: 3080953]

3. Harvey, P.J., Schoemaker, H.E. and Palmer, J.M. Veratryl alcohol as a mediator and the role of radical cations in lignin biodegradation by Phanerochaete chrysosporium, FEBS Lett. 195 (1986) 242-246.

4. Wariishi, H., Marquez, L., Dunford, H.B. and Gold, M.H. Lignin peroxidase compounds II and III. Spectral and kinetic characterization of reactions with peroxides. J. Biol. Chem. 265 (1990) 11137-11142. [PMID: 2162833]

5. Cai, D.Y. and Tien, M. Characterization of the oxycomplex of lignin peroxidases from Phanerochaete chrysosporium: equilibrium and kinetics studies. Biochemistry 29 (1990) 2085-2091. [PMID: 2328240]

6. Khindaria, A., Yamazaki, I. and Aust, S.D. Veratryl alcohol oxidation by lignin peroxidase. Biochemistry 34 (1995) 16860-16869. [PMID: 8527462]

7. Khindaria, A., Yamazaki, I. and Aust, S.D. Stabilization of the veratryl alcohol cation radical by lignin peroxidase. Biochemistry 35 (1996) 6418-6424. [PMID: 8639588]

8. Khindaria, A., Nie, G. and Aust, S.D. Detection and characterization of the lignin peroxidase compound II-veratryl alcohol cation radical complex. Biochemistry 36 (1997) 14181-14185. [PMID: 9369491]

9. Doyle, W.A., Blodig, W., Veitch, N.C., Piontek, K. and Smith, A.T. Two substrate interaction sites in lignin peroxidase revealed by site-directed mutagenesis. Biochemistry 37 (1998) 15097-15105. [PMID: 9790672]

10. Pollegioni, L., Tonin, F. and Rosini, E. Lignin-degrading enzymes. FEBS J. 282 (2015) 1190-1213. [PMID: 25649492]

[EC 1.11.1.14 created 1992, modified 2006, modified 2011, modified 2016]

EC 1.11.1.15

Accepted name: peroxiredoxin

Reaction: 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH

For diagram click here

Other name(s): thioredoxin peroxidase; tryparedoxin peroxidase; alkyl hydroperoxide reductase C22; AhpC; TrxPx; TXNPx; Prx; PRDX

Systematic name: thiol-containing-reductant:hydroperoxide oxidoreductase

Comments: Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins [1]. The peroxidase reaction comprises two steps centred around a redox-active cysteine called the peroxidatic cysteine. All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid) (see mechanism). The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), completing the catalytic cycle. In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond [1]. To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor [3]. The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule [4].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 207137-51-7

References:

1. Wood, Z.A., Schröder, E., Harris, J.R. and Poole, L.B. Structure, mechanism and regulation of peroxiredoxins. Trends Biochem. Sci. 28 (2003) 32-40. [PMID: 12517450]

2. Hofmann, B., Hecht, H.J. and Flohé, L. Peroxiredoxins. Biol. Chem. 383 (2002) 347-364. [PMID: 12033427]

3. Seo, M.S., Kang, S.W., Kim, K., Baines, I.C., Lee, T.H. and Rhee, S.G. Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate. J. Biol. Chem. 275 (2000) 20346-20354. [PMID: 10751410]

4. Choi, H.J., Kang, S.W., Yang, C.H., Rhee, S.G. and Ryu, S.E. Crystal structure of a novel human peroxidase enzyme at 2.0 Å resolution. Nat. Struct. Biol. 5 (1998) 400-406. [PMID: 9587003]

[EC 1.11.1.15 created 2004]

EC 1.11.1.16

Accepted name: versatile peroxidase

Reaction: (1) 1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O
(2) 2 manganese(II) + 2 H+ + H2O2 = 2 manganese(III) + 2 H2O

Glossary: 4-hydroxy-3-methoxybenzaldehyde = vanillin
2-methoxyphenol = guaiacol

Other name(s): VP; hybrid peroxidase; polyvalent peroxidase; reactive-black-5:hydrogen-peroxide oxidoreductase

Systematic name: 1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol:hydrogen-peroxide oxidoreductase

Comments: A hemoprotein. This ligninolytic peroxidase combines the substrate-specificity characteristics of the two other ligninolytic peroxidases, EC 1.11.1.13, manganese peroxidase and EC 1.11.1.14, lignin peroxidase. Unlike these two enzymes, it is also able to oxidize phenols, hydroquinones and both low- and high-redox-potential dyes, due to a hybrid molecular architecture that involves multiple binding sites for substrates [2,4].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 42613-30-9, 114995-15-2

References:

1. Martínez, M.J., Ruiz-Dueñas, F.J., Guillén, F. and Martínez, A.T. Purification and catalytic properties of two manganese peroxidase isoenzymes from Pleurotus eryngii, Eur. J. Biochem. 237 (1996) 424-432. [PMID: 8647081]

2. Heinfling, A., Ruiz-Dueñas, F.J., Martínez, M.J., Bergbauer, M., Szewzyk, U. and Martínez, A.T. A study on reducing substrates of manganese-oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta, FEBS Lett. 428 (1998) 141-146. [PMID: 9654123]

3. Ruiz-Dueñas, F.J., Martínez, M.J. and Martínez, A.T. Molecular characterization of a novel peroxidase isolated from the ligninolytic fungus Pleurotus eryngii, Mol. Microbiol. 31 (1999) 223-235. [PMID: 9987124]

4. Camarero, S., Sarkar, S., Ruiz-Dueñas, F.J., Martínez, M.J. and Martínez, A.T. Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites. J. Biol. Chem. 274 (1999) 10324-10330. [PMID: 10187820]

5. Ruiz-Dueñas, F.J., Martínez, M.J. and Martínez, A.T. Heterologous expression of Pleurotus eryngii peroxidase confirms its ability to oxidize Mn2+ and different aromatic substrates. Appl. Environ. Microbiol. 65 (1999) 4705-4707. [PMID: 10508113]

6. Camarero, S., Ruiz-Dueñas, F.J., Sarkar, S., Martínez, M.J. and Martínez, A.T. The cloning of a new peroxidase found in lignocellulose cultures of Pleurotus eryngii and sequence comparison with other fungal peroxidases. FEMS Microbiol. Lett. 191 (2000) 37-43. [PMID: 11004397]

7. Ruiz-Dueñas, F.J., Camarero, S., Pérez-Boada, M., Martínez, M.J. and Martínez, A.T. A new versatile peroxidase from Pleurotus, Biochem. Soc. Trans. 29 (2001) 116-122. [PMID: 11356138]

8. Banci, L., Camarero, S., Martínez, A.T., Martínez, M.J., Pérez-Boada, M., Pierattelli, R. and Ruiz-Dueñas, F.J. NMR study of manganese(II) binding by a new versatile peroxidase from the white-rot fungus Pleurotus eryngii, J. Biol. Inorg. Chem. 8 (2003) 751-760. [PMID: 12884090]

9. Pérez-Boada, M., Ruiz-Dueñas, F.J., Pogni, R., Basosi, R., Choinowski, T., Martínez, M.J., Piontek, K. and Martínez, A.T. Versatile peroxidase oxidation of high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and crystallographic investigation of three long-range electron transfer pathways. J. Mol. Biol. 354 (2005) 385-402. [PMID: 16246366]

10. Caramelo, L., Martínez, M.J. and Martínez, A.T. A search for ligninolytic peroxidases in the fungus Pleurotus eryngii involving α-keto-γ-thiomethylbutyric acid and lignin model dimer. Appl. Environ. Microbiol. 65 (1999) 916-922. [PMID: 10049842]

[EC 1.11.1.16 created 2006, modified 2016]

EC 1.11.1.17

Accepted name: glutathione amide-dependent peroxidase

Reaction: 2 glutathione amide + H2O2 = glutathione amide disulfide + 2 H2O

Systematic name: glutathione amide:hydrogen-peroxide oxidoreductase

Comments: This enzyme, which has been characterized from the proteobacterium Marichromatium gracile, is a chimeric protein, containing a peroxiredoxin-like N-terminus and a glutaredoxin-like C terminus. The enzyme has peroxidase activity towards hydrogen peroxide and several small alkyl hydroperoxides, and is thought to represent an early adaptation for fighting oxidative stress [1]. The glutathione amide disulfide produced by this enzyme can be restored to glutathione amide by EC 1.8.1.16 (glutathione amide reductase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Vergauwen, B., Pauwels, F., Jacquemotte, F., Meyer, T.E., Cusanovich, M.A., Bartsch, R.G. and Van Beeumen, J.J. Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling. J. Biol. Chem. 276 (2001) 20890-20897. [PMID: 11399772]

[EC 1.11.1.17 created 2010]

EC 1.11.1.18

Accepted name: bromide peroxidase

Reaction: RH + HBr + H2O2 = RBr + 2 H2O

Other name(s): bromoperoxidase; haloperoxidase (ambiguous); eosinophil peroxidase

Systematic name: bromide:hydrogen-peroxide oxidoreductase

Comments: Bromoperoxidases of red and brown marine algae (Rhodophyta and Phaeophyta) contain vanadate. They catalyse the bromination of a range of organic molecules such as sesquiterpenes, forming stable C-Br bonds. Bromoperoxidases also oxidize iodides.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. De Boer, E., Tromp, M.G.M., Plat, H., Krenn, G.E. and Wever, R Vanadium(v) as an essential element for haloperoxidase activity in marine brown-algae - purification and characterization of a vanadium(V)-containing bromoperoxidase from Laminaria saccharina. Biochim. Biophys. Acta 872 (1986) 104-115.

2. Tromp, M.G., Olafsson, G., Krenn, B.E. and Wever, R. Some structural aspects of vanadium bromoperoxidase from Ascophyllum nodosum. Biochim. Biophys. Acta 1040 (1990) 192-198. [PMID: 2400770]

3. Isupov, M.N., Dalby, A.R., Brindley, A.A., Izumi, Y., Tanabe, T., Murshudov, G.N. and Littlechild, J.A. Crystal structure of dodecameric vanadium-dependent bromoperoxidase from the red algae Corallina officinalis. J. Mol. Biol. 299 (2000) 1035-1049. [PMID: 10843856]

4. Carter-Franklin, J.N. and Butler, A. Vanadium bromoperoxidase-catalyzed biosynthesis of halogenated marine natural products. J. Am. Chem. Soc. 126 (2004) 15060-15066. [PMID: 15548002]

5. Ohshiro, T., Littlechild, J., Garcia-Rodriguez, E., Isupov, M.N., Iida, Y., Kobayashi, T. and Izumi, Y. Modification of halogen specificity of a vanadium-dependent bromoperoxidase. Protein Sci. 13 (2004) 1566-1571. [PMID: 15133166]

[EC 1.11.1.18 created 2010]

EC 1.11.1.19

Accepted name: dye decolorizing peroxidase

Reaction: Reactive Blue 5 + 2 H2O2 = phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O

Glossary: Reactive Blue 5 = 1-amino-4-{[3-({4-chloro-6-[(3-sulfophenyl)amino]-1,3,5-triazin-2-yl}amino)-4-sulfophenyl]amino}-9,10-dihydro-9,10-dioxoanthracene-2-sulfonic acid

Other name(s): DyP; DyP-type peroxidase

Systematic name: Reactive-Blue-5:hydrogen-peroxide oxidoreductase

Comments: Heme proteins with proximal histidine secreted by basidiomycetous fungi and eubacteria. They are similar to EC 1.11.1.16 versatile peroxidase (oxidation of Reactive Black 5, phenols, veratryl alcohol), but differ from the latter in their ability to efficiently oxidize a number of recalcitrant anthraquinone dyes, and inability to oxidize Mn(II). The model substrate Reactive Blue 5 is converted with high efficiency via a so far unique mechanism that combines oxidative and hydrolytic steps and leads to the formation of phthalic acid. Bacterial TfuDyP catalyses sulfoxidation.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc

References:

1. Kim, S.J. and Shoda, M. Purification and characterization of a novel peroxidase from Geotrichum candidum dec 1 involved in decolorization of dyes. Appl. Environ. Microbiol. 65 (1999) 1029-1035. [PMID: 10049859]

2. Sugano, Y., Ishii, Y. and Shoda, M. Role of H164 in a unique dye-decolorizing heme peroxidase DyP. Biochem. Biophys. Res. Commun. 322 (2004) 126-132. [PMID: 15313183]

3. Zubieta, C., Joseph, R., Krishna, S.S., McMullan, D., Kapoor, M., Axelrod, H.L., Miller, M.D., Abdubek, P., Acosta, C., Astakhova, T., Carlton, D., Chiu, H.J., Clayton, T., Deller, M.C., Duan, L., Elias, Y., Elsliger, M.A., Feuerhelm, J., Grzechnik, S.K., Hale, J., Han, G.W., Jaroszewski, L., Jin, K.K., Klock, H.E., Knuth, M.W., Kozbial, P., Kumar, A., Marciano, D., Morse, A.T., Murphy, K.D., Nigoghossian, E., Okach, L., Oommachen, S., Reyes, R., Rife, C.L., Schimmel, P., Trout, C.V., van den Bedem, H., Weekes, D., White, A., Xu, Q., Hodgson, K.O., Wooley, J., Deacon, A.M., Godzik, A., Lesley, S.A. and Wilson, I.A. Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA. Proteins 69 (2007) 234-243. [PMID: 17654547]

4. Sugano, Y., Matsushima, Y., Tsuchiya, K., Aoki, H., Hirai, M. and Shoda, M. Degradation pathway of an anthraquinone dye catalyzed by a unique peroxidase DyP from Thanatephorus cucumeris Dec 1. Biodegradation 20 (2009) 433-440. [PMID: 19009358]

5. Sugano, Y. DyP-type peroxidases comprise a novel heme peroxidase family. Cell. Mol. Life Sci. 66 (2009) 1387-1403. [PMID: 19099183]

6. Ogola, H.J., Kamiike, T., Hashimoto, N., Ashida, H., Ishikawa, T., Shibata, H. and Sawa, Y. Molecular characterization of a novel peroxidase from the cyanobacterium Anabaena sp. strain PCC 7120. Appl. Environ. Microbiol. 75 (2009) 7509-7518. [PMID: 19801472]

7. van Bloois, E., Torres Pazmino, D.E., Winter, R.T. and Fraaije, M.W. A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily. Appl. Microbiol. Biotechnol. 86 (2010) 1419-1430. [PMID: 19967355]

8. Liers, C., Bobeth, C., Pecyna, M., Ullrich, R. and Hofrichter, M. DyP-like peroxidases of the jelly fungus Auricularia auricula-judae oxidize nonphenolic lignin model compounds and high-redox potential dyes. Appl. Microbiol. Biotechnol. 85 (2010) 1869-1879. [PMID: 19756587]

9. Hofrichter, M., Ullrich, R., Pecyna, M.J., Liers, C. and Lundell, T. New and classic families of secreted fungal heme peroxidases. Appl. Microbiol. Biotechnol. 87 (2010) 871-897. [PMID: 20495915]

[EC 1.11.1.19 created 2011, modified 2015]

EC 1.11.1.20

Accepted name: prostamide/prostaglandin F synthase

Reaction: thioredoxin + (5Z,9α,11α,13E,15S)-9,11-epidioxy-15-hydroxy-prosta-5,13-dienoate = thioredoxin disulfide + (5Z,9α,11α,13E,15S)-9,11,15-trihydroxyprosta-5,13-dienoate

Glossary: prostamide H2 = (5Z)-N-(2-hydroxyethyl)-7-{(1R,4S,5R,6R)-6-[(1E,3S)-3-hydroxyoct-1-en-1-yl]-2,3-dioxabicyclo[2.2.1]hept-5-yl}hept-5-enamide
prostamide F = (5Z,9α,11α,13E,15S)-9,11,15-trihydroxy-N-(2-hydroxyethyl)prosta-5,13-dien-1-amide
prostaglandin H2 = (5Z,9α,11α,13E,15S)-9,11-epidioxy-15-hydroxy-prosta-5,13-dienoate
prostaglandin F = (5Z,9α,11α,13E,15S)-9,11,15-trihydroxyprosta-5,13-dienoate

Other name(s): prostamide/PGF synthase; prostamide F synthase; prostamide/prostaglandin F synthase; tPGF synthase

Systematic name: thioredoxin:(5Z,9α,11α,13E,15S)-9,11-epidioxy-15-hydroxy-prosta-5,13-dienoate oxidoreductase

Comments: The enzyme contains a thioredoxin-type disulfide as a catalytic group. Prostamide H2 and prostaglandin H2 are the best substrates; the latter is converted to prostaglandin F. The enzyme also reduces tert-butyl hydroperoxide, cumene hydroperoxide and H2O2, but not prostaglandin D2 or prostaglandin E2.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Moriuchi, H., Koda, N., Okuda-Ashitaka, E., Daiyasu, H., Ogasawara, K., Toh, H., Ito, S., Woodward, D.F. and Watanabe, K. Molecular characterization of a novel type of prostamide/prostaglandin F synthase, belonging to the thioredoxin-like superfamily. J. Biol. Chem. 283 (2008) 792-801. [PMID: 18006499]

2. Yoshikawa, K., Takei, S., Hasegawa-Ishii, S., Chiba, Y., Furukawa, A., Kawamura, N., Hosokawa, M., Woodward, D.F., Watanabe, K. and Shimada, A. Preferential localization of prostamide/prostaglandin F synthase in myelin sheaths of the central nervous system. Brain Res. 1367 (2011) 22-32. [PMID: 20950588]

[EC 1.11.1.20 created 2011]

EC 1.11.1.21

Accepted name: catalase-peroxidase

Reaction: (1) donor + H2O2 = oxidized donor + 2 H2O
(2) 2 H2O2 = O2 + 2 H2O

Other name(s): katG (gene name)

Systematic name: donor:hydrogen-peroxide oxidoreductase

Comments: Differs from EC 1.11.1.7, peroxidase in having a relatively high catalase (EC 1.11.1.6) activity with H2O2 as donor, releasing O2; both activities use the same heme active site. In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Loewen, P.C., Triggs, B.L., George, C.S. and Hrabarchuk, B.E. Genetic mapping of katG, a locus that affects synthesis of the bifunctional catalase-peroxidase hydroperoxidase I in Escherichia coli. J. Bacteriol. 162 (1985) 661-667. [PMID: 3886630]

2. Hochman, A. and Goldberg, I. Purification and characterization of a catalase-peroxidase and a typical catalase from the bacterium Klebsiella pneumoniae. Biochim. Biophys. Acta 1077 (1991) 299-307. [PMID: 2029529]

3. Fraaije, M.W., Roubroeks, H.P., van Berkel, W.H.J. Purification and characterization of an intracellular catalase-peroxidase from Penicillium simplicissimum. Eur. J. Biochem. 235 (1996) 192-198. [PMID: 8631329]

4. Bertrand, T., Eady, N.A., Jones, J.N., Jesmin, Nagy, J.M., Jamart-Gregoire, B., Raven, E.L. and Brown, K.A. Crystal structure of Mycobacterium tuberculosis catalase-peroxidase. J. Biol. Chem. 279 (2004) 38991-38999. [PMID: 15231843]

5. Vlasits, J., Jakopitsch, C., Bernroitner, M., Zamocky, M., Furtmuller, P.G. and Obinger, C. Mechanisms of catalase activity of heme peroxidases. Arch. Biochem. Biophys. 500 (2010) 74-81. [PMID: 20434429]

[EC 1.11.1.21 created 2011]

EC 1.11.1.22

Accepted name: hydroperoxy fatty acid reductase

Reaction: a hydroperoxy fatty acid + NADPH + H+ = a hydroxy fatty acid + NADP+ + H2O

Other name(s): slr1171 (gene name); slr1992 (gene name)

Systematic name: NADPH:hydroperoxy fatty acid oxidoreductase

Comments: The enzyme, characterized from the cyanobacterium Synechocystis PCC 6803, can reduce unsaturated fatty acid hydroperoxides and alkyl hydroperoxides. The enzyme, which utilizes NADPH generated by the photosynthetic electron transfer system, protects the cells from lipid peroxidation.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Gaber, A., Tamoi, M., Takeda, T., Nakano, Y. and Shigeoka, S. NADPH-dependent glutathione peroxidase-like proteins (Gpx-1, Gpx-2) reduce unsaturated fatty acid hydroperoxides in Synechocystis PCC 6803. FEBS Lett 499 (2001) 32-36. [PMID: 11418106]

2. Gaber, A., Yoshimura, K., Tamoi, M., Takeda, T., Nakano, Y. and Shigeoka, S. Induction and functional analysis of two reduced nicotinamide adenine dinucleotide phosphate-dependent glutathione peroxidase-like proteins in Synechocystis PCC 6803 during the progression of oxidative stress. Plant Physiol. 136 (2004) 2855-2861. [PMID: 15347790]

[EC 1.11.1.22 created 2013]

EC 1.11.1.23

Accepted name: (S)-2-hydroxypropylphosphonic acid epoxidase

Reaction: (S)-2-hydroxypropylphosphonate + H2O2 = (1R,2S)-1,2-epoxypropylphosphonate + 2 H2O

For diagram of reaction click here.

Glossary: (1R,2S)-1,2-epoxypropylphosphonate = fosfomycin = [(2R,3S)-3-methyloxiran-2-yl]phosphonate

Other name(s): HPP epoxidase; HppE; 2-hydroxypropylphosphonic acid epoxidase; Fom4; (S)-2-hydroxypropylphosphonate epoxidase

Systematic name: (S)-2-hydroxypropylphosphonate:hydrogen-peroxide epoxidase

Comments: This is the last enzyme in the biosynthetic pathway of fosfomycin, a broad-spectrum antibiotic produced by certain Streptomyces species. Contains non heme iron that forms a iron(IV)-oxo (ferryl) complex with hydrogen peroxide, which functions as a proton abstractor from the substrate [7].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Munos, J.W., Moon, S.J., Mansoorabadi, S.O., Chang, W., Hong, L., Yan, F., Liu, A. and Liu, H.W. Purification and characterization of the epoxidase catalyzing the formation of fosfomycin from Pseudomonas syringae. Biochemistry 47 (2008) 8726-8735. [PMID: 18656958]

2. Yan, F., Moon, S.J., Liu, P., Zhao, Z., Lipscomb, J.D., Liu, A. and Liu, H.W. Determination of the substrate binding mode to the active site iron of (S)-2-hydroxypropylphosphonic acid epoxidase using 17O-enriched substrates and substrate analogues. Biochemistry 46 (2007) 12628-12638. [PMID: 17927218]

3. Hidaka, T., Goda, M., Kuzuyama, T., Takei, N., Hidaka, M. and Seto, H. Cloning and nucleotide sequence of fosfomycin biosynthetic genes of Streptomyces wedmorensis. Mol. Gen. Genet. 249 (1995) 274-280. [PMID: 7500951]

4. Liu, P., Mehn, M.P., Yan, F., Zhao, Z., Que, L., Jr. and Liu, H.W. Oxygenase activity in the self-hydroxylation of (S)-2-hydroxypropylphosphonic acid epoxidase involved in fosfomycin biosynthesis. J. Am. Chem. Soc. 126 (2004) 10306-10312. [PMID: 15315444]

5. Higgins, L.J., Yan, F., Liu, P., Liu, H.W. and Drennan, C.L. Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme. Nature 437 (2005) 838-844. [PMID: 16015285]

6. Cameron, S., McLuskey, K., Chamberlayne, R., Hallyburton, I. and Hunter, W.N. Initiating a crystallographic analysis of recombinant (S)-2-hydroxypropylphosphonic acid epoxidase from Streptomyces wedmorensis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 (2005) 534-536. [PMID: 16511089]

7. Wang, C., Chang, W.C., Guo, Y., Huang, H., Peck, S.C., Pandelia, M.E., Lin, G.M., Liu, H.W., Krebs, C. and Bollinger, J.M., Jr. Evidence that the fosfomycin-producing epoxidase, HppE, is a non-heme-iron peroxidase. Science 342 (2013) 991-995. [PMID: 24114783]

[EC 1.11.1.23 created 2011 as EC 1.14.19.7, 2014 transferred to EC 1.11.1.23]


EC 1.11.2 With H2O2 as acceptor, one oxygen atom of which is incorporated into the product

Contents

EC 1.11.2.1 unspecific peroxygenase
EC 1.11.2.2 myeloperoxidase
EC 1.11.2.3 plant seed peroxygenase
EC 1.11.2.4 fatty-acid peroxygenase
EC 1.11.2.5 3-methyl-L-tyrosine peroxygenase

EC 1.11.2.1

Accepted name: unspecific peroxygenase

Reaction: RH + H2O2 = ROH + H2O

Other name(s): aromatic peroxygenase; mushroom peroxygenase; haloperoxidase-peroxygenase; Agrocybe aegerita peroxidase

Systematic name: substrate:hydrogen-peroxide oxidoreductase (RH-hydroxylating or -epoxidising)

Comments: A heme-thiolate protein (P450). Enzymes of this type include glycoproteins secreted by agaric basidiomycetes. They catalyse the insertion of an oxygen atom from H2O2 into a wide variety of substrates, including aromatic rings such as naphthalene, toluene, phenanthrene, pyrene and p-nitrophenol, recalcitrant heterocycles such as pyridine, dibenzofuran, various ethers (resulting in O-dealkylation) and alkanes such as propane, hexane and cyclohexane. Reactions catalysed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, O- and N-dealkylation, bromination and one-electron oxidations. They have little or no activity toward chloride. Mechanistically, the catalytic cycle of unspecific (mono)-peroxygenases combines elements of the "shunt" pathway of cytochrome P450s (a side activity that utilizes a peroxide in place of dioxygen and NAD[P]H) and the classic heme peroxidase cycle.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Ullrich, R., Nuske, J., Scheibner, K., Spantzel, J. and Hofrichter, M. Novel haloperoxidase from the agaric basidiomycete Agrocybe aegerita oxidizes aryl alcohols and aldehydes. Appl. Environ. Microbiol. 70 (2004) 4575-4581. [PMID: 15294788]

2. Ullrich, R. and Hofrichter, M. The haloperoxidase of the agaric fungus Agrocybe aegerita hydroxylates toluene and naphthalene. FEBS Lett. 579 (2005) 6247-6250. [PMID: 16253244]

3. Anh, D.H., Ullrich, R., Benndorf, D., Svatos, A., Muck, A. and Hofrichter, M. The coprophilous mushroom Coprinus radians secretes a haloperoxidase that catalyzes aromatic peroxygenation. Appl. Environ. Microbiol. 73 (2007) 5477-5485. [PMID: 17601809]

4. Aranda, E., Kinne, M., Kluge, M., Ullrich, R. and Hofrichter, M. Conversion of dibenzothiophene by the mushrooms Agrocybe aegerita and Coprinellus radians and their extracellular peroxygenases. Appl. Microbiol. Biotechnol. 82 (2009) 1057-1066. [PMID: 19039585]

5. Kinne, M., Poraj-Kobielska, M., Aranda, E., Ullrich, R., Hammel, K.E., Scheibner, K. and Hofrichter, M. Regioselective preparation of 5-hydroxypropranolol and 4'-hydroxydiclofenac with a fungal peroxygenase. Bioorg. Med. Chem. Lett. 19 (2009) 3085-3087. [PMID: 19394224]

6. Kluge, M., Ullrich, R., Dolge, C., Scheibner, K. and Hofrichter, M. Hydroxylation of naphthalene by aromatic peroxygenase from Agrocybe aegerita proceeds via oxygen transfer from H2O2 and intermediary epoxidation. Appl. Microbiol. Biotechnol. 81 (2009) 1071-1076. [PMID: 18815784]

7. Ullrich, R., Dolge, C., Kluge, M. and Hofrichter, M. Pyridine as novel substrate for regioselective oxygenation with aromatic peroxygenase from Agrocybe aegerita. FEBS Lett. 582 (2008) 4100-4106. [PMID: 19022254]

8. Aranda, E., Kinne, M., Kluge, M., Ullrich, R. and Hofrichter, M. Conversion of dibenzothiophene by the mushrooms Agrocybe aegerita and Coprinellus radians and their extracellular peroxygenases. Appl. Microbiol. Biotechnol. 82 (2009) 1057-1066. [PMID: 19039585]

9. Kinne, M., Poraj-Kobielska, M., Ralph, S.A., Ullrich, R., Hofrichter, M. and Hammel, K.E. Oxidative cleavage of diverse ethers by an extracellular fungal peroxygenase. J. Biol. Chem. 284 (2009) 29343-29349. [PMID: 19713216]

10. Pecyna, M.J., Ullrich, R., Bittner, B., Clemens, A., Scheibner, K., Schubert, R. and Hofrichter, M. Molecular characterization of aromatic peroxygenase from Agrocybe aegerita. Appl. Microbiol. Biotechnol. 84 (2009) 885-897. [PMID: 19434406]

[EC 1.11.2.1 created 2011]

EC 1.11.2.2

Accepted name: myeloperoxidase

Reaction: Cl + H2O2 + H+ = HClO + H2O

Other name(s): MPO; verdoperoxidase

Systematic name: chloride:hydrogen-peroxide oxidoreductase (hypochlorite-forming)

Comments: Contains calcium and covalently bound heme (proximal ligand histidine). It is present in phagosomes of neutrophils and monocytes, where the hypochlorite produced is strongly bactericidal. It differs from EC 1.11.1.10 chloride peroxidase in its preference for formation of hypochlorite over the chlorination of organic substrates under physiological conditions (pH 5-8). Hypochlorite in turn forms a number of antimicrobial products (Cl2, chloramines, hydroxyl radical, singlet oxygen). MPO also oxidizes bromide, iodide and thiocyanate. In the absence of halides, it oxidizes phenols and has a moderate peroxygenase activity toward styrene.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Agner, K. Myeloperoxidase. Advances in Enzymology 3 (1943) 137-148.

2. Harrison, J.E. and Schultz, J. Studies on the chlorinating activity of myeloperoxidase. J. Biol. Chem. 251 (1976) 1371-1374. [PMID: 176150]

3. Furtmuller, P.G., Burner, U. and Obinger, C. Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate. Biochemistry 37 (1998) 17923-17930. [PMID: 9922160]

4. Tuynman, A., Spelberg, J.L., Kooter, I.M., Schoemaker, H.E. and Wever, R. Enantioselective epoxidation and carbon-carbon bond cleavage catalyzed by Coprinus cinereus peroxidase and myeloperoxidase. J. Biol. Chem. 275 (2000) 3025-3030. [PMID: 10652281]

5. Klebanoff, S.J. Myeloperoxidase: friend and foe. J Leukoc Biol 77 (2005) 598-625. [PMID: 15689384]

6. Fiedler, T.J., Davey, C.A. and Fenna, R.E. X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 Å resolution. J. Biol. Chem. 275 (2000) 11964-11971. [PMID: 10766826]

7. Gaut, J.P., Yeh, G.C., Tran, H.D., Byun, J., Henderson, J.P., Richter, G.M., Brennan, M.L., Lusis, A.J., Belaaouaj, A., Hotchkiss, R.S. and Heinecke, J.W. Neutrophils employ the myeloperoxidase system to generate antimicrobial brominating and chlorinating oxidants during sepsis. Proc. Natl. Acad. Sci. USA 98 (2001) 11961-11966. [PMID: 11593004]

[EC 1.11.2.2 created 2011]

EC 1.11.2.3

Accepted name: plant seed peroxygenase

Reaction: R1H + R2OOH = R1OH + R2OH

Other name(s): plant peroxygenase, soybean peroxygenase

Systematic name: substrate:hydroperoxide oxidoreductase (RH-hydroxylating or epoxidising)

Comments: A heme protein with calcium binding motif (caleosin-type). Enzymes of this type include membrane-bound proteins found in seeds of different plants. They catalyse the direct transfer of one oxygen atom from an organic hydroperoxide, which is reduced into its corresponding alcohol to a substrate which will be oxidized. Reactions catalysed include hydroxylation, epoxidation and sulfoxidation. Preferred substrate and co-substrate are unsaturated fatty acids and fatty acid hydroperoxides, respectively. Plant seed peroxygenase is involved in the synthesis of cutin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Ishimaru, A. Purification and characterization of solubilized peroxygenase from microsomes of pea seeds. J. Biol. Chem. 254 (1979) 8427-8433. [PMID: 468835]

2. Blee, E., Wilcox, A.L., Marnett, L.J. and Schuber, F. Mechanism of reaction of fatty acid hydroperoxides with soybean peroxygenase. J. Biol. Chem. 268 (1993) 1708-1715. [PMID: 8420948]

3. Hamberg, M. and Hamberg, G. Peroxygenase-catalyzed fatty acid epoxidation in cereal seeds (sequential oxidation of linoleic acid into 9(S),12(S),13(S)-trihydroxy-10(E)-octadecenoic acid). Plant Physiol. 110 (1996) 807-815. [PMID: 12226220]

4. Lequeu, J., Fauconnier, M.L., Chammai, A., Bronner, R. and Blee, E. Formation of plant cuticle: evidence for the occurrence of the peroxygenase pathway. Plant J. 36 (2003) 155-164. [PMID: 14535881]

5. Hanano, A., Burcklen, M., Flenet, M., Ivancich, A., Louwagie, M., Garin, J. and Blee, E. Plant seed peroxygenase is an original heme-oxygenase with an EF-hand calcium binding motif. J. Biol. Chem. 281 (2006) 33140-33151. [PMID: 16956885]

[EC 1.11.2.3 created 2011]

EC 1.11.2.4

Accepted name: fatty-acid peroxygenase

Reaction: fatty acid + H2O2 = 3- or 2-hydroxy fatty acid + H2O

Other name(s): fatty acid hydroxylase; P450 peroxygenase; CYP152A1; P450BS; P450SPα

Systematic name: fatty acid:hydroperoxide oxidoreductase (RH-hydroxylating)

Comments: A cytosolic heme-thiolate protein with sequence homology to P450 monooxygenases. Unlike the latter, it needs neither NAD(P)H, dioxygen nor specific reductases for function. Enzymes of this type are produced by bacteria (e.g. Sphingomonas paucimobilis. Bacillus subtilis). Catalytic turnover rates are high compared with those of monooxygenation reactions as well as peroxide shunt reactions catalysed by the common P450s. A model substrate is myristate, but other saturated and unsaturated fatty acids are also hydroxylated. Oxidizes the peroxidase substrate 3,3',5,5'-tetramethylbenzidine (TMB) and peroxygenates aromatic substrates in a fatty-acid-dependent reaction.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Matsunaga, I., Yamada, M., Kusunose, E., Nishiuchi, Y., Yano, I. and Ichihara, K. Direct involvement of hydrogen peroxide in bacterial α-hydroxylation of fatty acid. FEBS Lett. 386 (1996) 252-254. [PMID: 8647293]

2. Matsunaga, I., Yamada, M., Kusunose, E., Miki, T. and Ichihara, K. Further characterization of hydrogen peroxide-dependent fatty acid α-hydroxylase from Sphingomonas paucimobilis. J. Biochem. 124 (1998) 105-110. [PMID: 9644252]

3. Matsunaga, I., Ueda, A., Fujiwara, N., Sumimoto, T. and Ichihara, K. Characterization of the ybdT gene product of Bacillus subtilis: novel fatty acid β-hydroxylating cytochrome P450. Lipids 34 (1999) 841-846. [PMID: 10529095]

4. Imai, Y., Matsunaga, I., Kusunose, E. and Ichihara, K. Unique heme environment at the putative distal region of hydrogen peroxide-dependent fatty acid α-hydroxylase from Sphingomonas paucimobilis (peroxygenase P450SPα). J. Biochem. 128 (2000) 189-194. [PMID: 10920253]

5. Matsunaga, I., Yamada, A., Lee, D.S., Obayashi, E., Fujiwara, N., Kobayashi, K., Ogura, H. and Shiro, Y. Enzymatic reaction of hydrogen peroxide-dependent peroxygenase cytochrome P450s: kinetic deuterium isotope effects and analyses by resonance Raman spectroscopy. Biochemistry 41 (2002) 1886-1892. [PMID: 11827534]

6. Lee, D.S., Yamada, A., Sugimoto, H., Matsunaga, I., Ogura, H., Ichihara, K., Adachi, S., Park, S.Y. and Shiro, Y. Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies. J. Biol. Chem. 278 (2003) 9761-9767. [PMID: 12519760]

7. Matsunaga, I. and Shiro, Y. Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes. Curr. Opin. Chem. Biol. 8 (2004) 127-132. [PMID: 15062772]

8. Shoji, O., Wiese, C., Fujishiro, T., Shirataki, C., Wunsch, B. and Watanabe, Y. Aromatic C-H bond hydroxylation by P450 peroxygenases: a facile colorimetric assay for monooxygenation activities of enzymes based on Russig’s blue formation. J. Biol. Inorg. Chem. 15 (2010) 1109-1115. [PMID: 20490877]

[EC 1.11.2.4 created 2011]

EC 1.11.2.5

Accepted name: 3-methyl-L-tyrosine peroxygenase

Reaction: 3-methyl-L-tyrosine + H2O2 = 3-hydroxy-5-methyl-L-tyrosine + H2O

For diagram of reaction click here.

Other name(s): SfmD; SacD; 3-methyltyrosine peroxidase; 3-methyl-L-tyrosine peroxidase

Systematic name: 3-methyl-L-tyrosine:hydrogen-peroxide oxidoreductase (3-hydroxy-5-methyl-L-tyrosine-forming)

Comments: The heme-containing peroxygenase from the bacterium Streptomyces lavendulae is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Tang, M.C., Fu, C.Y. and Tang, G.L. Characterization of SfmD as a heme peroxidase that catalyzes the regioselective hydroxylation of 3-methyltyrosine to 3-hydroxy-5-methyltyrosine in saframycin A biosynthesis. J. Biol. Chem. 287 (2012) 5112-5121. [PMID: 22187429]

[EC 1.11.2.5 created 2014]

EC 1.12 ACTING ON HYDROGEN AS DONORS

Sections

EC 1.12.1 With NAD+ or NADP+ as acceptor
EC 1.12.2 With a cytochrome as acceptor
EC 1.12.7 With a iron-sulfur protein as acceptor
EC 1.12.99 With other acceptors

EC 1.12.1 With NAD+ or NADP+ as acceptor

Contents

EC 1.12.1.1 now EC 1.18.99.1
EC 1.12.1.2 hydrogen dehydrogenase
EC 1.12.1.3 hydrogen dehydrogenase (NADP+)
EC 1.12.1.4 hydrogenase (NAD+, ferredoxin)
EC 1.12.1.5 hydrogen dehydrogenase [NAD(P)+]

[EC 1.12.1.1 Transferred entry: now EC 1.18.99.1 hydrogenase (EC 1.12.1.1 created 1965, deleted 1972)]

EC 1.12.1.2

Accepted name: hydrogen dehydrogenase

Reaction: H2 + NAD+ = H+ + NADH

Other name(s): H2:NAD+ oxidoreductase; NAD-linked hydrogenase; bidirectional hydrogenase; hydrogenase

Systematic name: hydrogen:NAD+ oxidoreductase

Comments: An iron-sulfur flavoprotein (FMN or FAD). Some forms of this enzyme contain nickel.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 9027-05-8

References:

1. Bone, D.H., Bernstein, S. and Vishniac, W. Purification and some properties of different forms of hydrogen dehydrogenase. Biochim. Biophys. Acta 67 (1963) 581-588.

2. Schneider, K. and Schlegel, H.G. Purification and properties of soluble hydrogenase from Alcaligenes eutrophus H 16. Biochim. Biophys. Acta 452 (1976) 66-80. [PMID: 186126]

[EC 1.12.1.2 created 1972, modified 2002]

EC 1.12.1.3

Accepted name: hydrogen dehydrogenase (NADP+)

Reaction: H2 + NADP+ = H+ + NADPH

Other name(s): NADP+-linked hydrogenase; NADP+-reducing hydrogenase; hydrogenase (ambiguous); hydrogenase I (ambiguous)

Systematic name: hydrogen:NADP+ oxidoreductase

Comments: The protein from the bacterium Desulfovibrio fructosovorans is an iron-sulfur protein that exclusively functions as a hydrogen dehydrogenase [1], while the enzyme from the archaeon Pyrococcus furiosus is a nickel, iron, iron-sulfur protein, that is part of a heterotetrameric complex where the α and δ subunits function as a hydrogenase while the β and γ subunits function as sulfur reductase (EC 1.12.98.4, sulfhydrogenase). Different from EC 1.12.1.5, hydrogen dehydrogenase [NAD(P)+].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9027-05-8

References:

1. de Luca, G., de Philip, P., Rousset, M., Belaich, J.P. and Dermoun, Z. The NADP-reducing hydrogenase of Desulfovibrio fructosovorans: Evidence for a native complex with hydrogen-dependent methyl-viologen-reducing activity. Biochem. Biophys. Res. Commun. 248 (1998) 591-596. [PMID: 9703971]

2. Bryant, F.O. and Adams, M.W. Characterization of hydrogenase from the hyperthermophilic archaebacterium, Pyrococcus furiosus. J. Biol. Chem. 264 (1989) 5070-5079. [PMID: 2538471]

3. Ma, K., Schicho, R.N., Kelly, R.M. and Adams, M.W. Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: evidence for a sulfur-reducing hydrogenase ancestor. Proc. Natl. Acad. Sci. USA 90 (1993) 5341-5344. [PMID: 8389482]

4. Ma, K., Zhou, Z.H. and Adams, M.W. Hydrogen production from pyruvate by enzymes purified from the hyperthermophilic archaeon, Pyrococcus furiosus: A key role for NADPH. FEMS Microbiol. Lett. 122 (1994) 245-250.

5. van Haaster, D.J., Silva, P.J., Hagedoorn, P.L., Jongejan, J.A. and Hagen, W.R. Reinvestigation of the steady-state kinetics and physiological function of the soluble NiFe-hydrogenase I of Pyrococcus furiosus. J. Bacteriol. 190 (2008) 1584-1587. [PMID: 18156274]

[EC 1.12.1.3 created 2002, modified 2013]

EC 1.12.1.4

Accepted name: hydrogenase (NAD+, ferredoxin)

Reaction: 2 H2 + NAD+ + 2 oxidized ferredoxin = 5 H+ + NADH + 2 reduced ferredoxin

Other name(s): bifurcating [FeFe] hydrogenase

Systematic name: hydrogen:NAD+, ferredoxin oxidoreductase

Comments: The enzyme from Thermotoga maritima contains a [FeFe] cluster (H-cluster) and iron-sulfur clusters. It works in the direction evolving hydrogen as a means of eliminating excess reducing equivalents.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Verhagen, M.F., O'Rourke, T. and Adams, M.W. The hyperthermophilic bacterium, Thermotoga maritima, contains an unusually complex iron-hydrogenase: amino acid sequence analyses versus biochemical characterization. Biochim. Biophys. Acta 1412 (1999) 212-229. [PMID: 10482784]

2. Schut, G.J. and Adams, M.W. The iron-hydrogenase of Thermotoga maritima utilizes ferredoxin and NADH synergistically: a new perspective on anaerobic hydrogen production. J. Bacteriol. 191 (2009) 4451-4457. [PMID: 19411328]

[EC 1.12.1.4 created 2011]

EC 1.12.1.5

Accepted name: hydrogen dehydrogenase [NAD(P)+]

Reaction: H2 + NAD(P)+ = H+ + NAD(P)H

Other name(s): hydrogenase II (ambiguous)

Systematic name: hydrogen:NAD(P)+ oxidoreductase

Comments: A nickel, iron, iron-sulfur protein. The enzyme from the archaeon Pyrococcus furiosus is part of a heterotetrameric complex where the α and δ subunits function as a hydrogenase while the β and γ subunits function as sulfur reductase (EC 1.12.98.4, sulfhydrogenase). Different from EC 1.12.1.3, hydrogen dehydrogenase (NADP+).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Ma, K., Weiss, R. and Adams, M.W. Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction. J. Bacteriol. 182 (2000) 1864-1871. [PMID: 10714990]

[EC 1.12.1.5 created 2013]


EC 1.12.2 With cytochrome as acceptor

EC 1.12.2.1

Accepted name: cytochrome-c3 hydrogenase

Reaction: 2 H2 + ferricytochrome c3 = 4 H+ + ferrocytochrome c3

Other name(s): H2:ferricytochrome c3 oxidoreductase; cytochrome c3 reductase; cytochrome hydrogenase; hydrogenase [ambiguous]

Systematic name: hydrogen:ferricytochrome-c3 oxidoreductase

Comments: An iron-sulfur protein. Some forms of the enzyme contain nickel ([NiFe]-hydrogenases) and, of these, some contain selenocysteine ([NiFeSe]-hydrogenases). Methylene blue and other acceptors can also be reduced.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD , CAS registry number: 9027-05-8

References:

1. DerVartanian, D.V. and Le Gall, J. A monomolecular electron transfer chain: structure and function of cytochrome c3. Biochim. Biophys. Acta 346 (1974) 79-99.

2. Higuchi, Y., Yasuoka, N., Kakudo, M., Katsube, Y., Yagi, T. and Inokuchi, H. Single crystals of hydrogenase from Desulfovibrio vulgaris Miyazaki F. J. Biol. Chem. 262 (1987) 2823-2825. [PMID: 3546297]

3. Rilkis, E. and Rittenberg, D. Some observations on the enzyme, hydrogenase. J. Biol. Chem. 236 (1961) 2526-2529.

4. Sadana, J.C. and Morey, A.V. Purification and properties of the hydrogenase of Desulfovibrio desulfuricans. Biochim. Biophys. Acta 50 (1961) 153-163.

5. Volbeda, A., Charon, M.H., Piras, C., Hatchikian, E.C., Frey, M. and Fontecillacamps, J.C. Crystal-structure of the nickel-iron hydrogenase from Desulfovibrio gigas. Nature 373 (1995) 580-587. [PMID: 7854413]

6. Garcin, E., Vernede, X., Hatchikian, E.C., Volbeda, A., Frey, M. and Fontecilla-Camps, J.C. The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center. Structure Fold. Des. 7 (1999) 557-566. [PMID: 10378275]

[EC 1.12.2.1 created 1972, modified 2002]


EC 1.12.5 With a quinone or similar compound as acceptor

EC 1.12.5.1

Accepted name: hydrogen:quinone oxidoreductase

Reaction: H2 + menaquinone = menaquinol

Other name(s): hydrogen-ubiquinone oxidoreductase; hydrogen:menaquinone oxidoreductase; membrane-bound hydrogenase; quinone-reactive Ni/Fe-hydrogenase

Systematic name: hydrogen:quinone oxidoreductase

Comments: Contains nickel, iron-sulfur clusters and cytochrome b. Also catalyses the reduction of water-soluble quinones (e.g. 2,3-dimethylnaphthoquinone) or viologen dyes (benzyl viologen or methyl viologen).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 151616-65-8

References:

1. Dross, F., Geisler, V., Lenger, R., Theis, F., Krafft, T., Fahrenholz, F., Kojro, E., Duchêne, A., Tripier, D., Juvenal, K. and Kröger, A. The quinone-reactive Ni/Fe-hydrogenase of Wolinella succinogenes. Eur. J. Biochem. 206 (1992) 93-102. [PMID: 1587288]

2. Dross, F., Geisler, V., Lenger, R., Theis, F., Krafft, T., Fahrenholz, F., Kojro, E., Duchêne, A., Tripier, D., Juvenal, K. and Kröger, A. The quinone-reactive Ni/Fe-hydrogenase of Wolinella succinogenes. Eur. J. Biochem. 206 (1992) 93-102. [PMID: 92267032] [An erratum appears in Eur. J. Biochem. 214 (1993) 949-050 [PMID: 8319698].

3. Gross, R., Simon, J., Lancaster, C.R.D. and Kroger, A. Identification of histidine residues in Wolinella succinogenes hydrogenase that are essential for menaquinone reduction by H-2. Mol. Microbiol. 30 (1998) 639-646. [PMID: 9822828]

4. Bernhard, M., Benelli, B., Hochkoeppler, A., Zannoni, D. and Friedrich, B. Functional and structural role of the cytochrome b subunit of the membrane-bound hydrogenase complex of Alcaligenes eutrophus H16. Eur. J. Biochem. 248 (1997) 179-186. [PMID: 9310376]

5. Ferber, D.M. and Maier, R.J. Hydrogen-ubiquinone oxidoreductase activity by the Bradyrhizobium japonicum membrane-bound hydrogenase. FEMS Microbiol. Lett. 110 (1993) 257-264. [PMID: 8354459]

6. Ishii, M., Omori, T., Igarashi, Y., Adachi, O., Ameyama, M. and Kodama, T. Methionaquinone is a direct natural electron-acceptor for the membrane-bound hydrogenase in Hydrogenobacter thermophilus strain TK-6. Agric. Biol. Chem. 55 (1991) 3011-3016.

[EC 1.12.5.1 created 1999 as EC 1.12.99.3, transferred 2002 to EC 1.12.5.1]


EC 1.12.7 With an iron-sulfur protein as acceptor

Contents

EC 1.12.7.1 now EC 1.18.99.1
EC 1.12.7.2 ferredoxin hydrogenase

[EC 1.12.7.1 Transferred entry: now EC 1.18.99.1 hydrogenase (EC 1.12.7.1 created 1972, deleted 1978)]

EC 1.12.7.2

Accepted name: ferredoxin hydrogenase

Reaction: H2 + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H+

Other name(s): H2 oxidizing hydrogenase; H2 producing hydrogenase [ambiguous]; bidirectional hydrogenase; hydrogen-lyase [ambiguous]; hydrogenase (ferredoxin); hydrogenase I; hydrogenase II; hydrogenlyase [ambiguous]; uptake hydrogenase [ambiguous]

Systematic name: hydrogen:ferredoxin oxidoreductase

Comments: Contains iron-sulfur clusters. The enzymes from some sources contains nickel. Can use molecular hydrogen for the reduction of a variety of substances. Formerly EC 1.12.1.1, EC 1.12.7.1, EC 1.98.1.1, EC 1.18.3.1 and EC 1.18.99.1.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9027-05-8

References:

1. Shug, A.L., Wilson, P.W., Green, D.E. and Mahler, H.R. The role of molybdenum and flavin in hydrogenase. J. Am. Chem. Soc. 76 (1954) 3355-3356.

2. Tagawa, K. and Arnon, D.I. Ferredoxin as electron carriers in photosynthesis and in the bioogical production and consumption of hydrogen gas. Nature (Lond.) 195 (1962) 537-543.

3. Valentine, R.C., Mortenson, L.E. and Carnahan, J.E. The hydrogenase system of Clostridium pasteurianum. J. Biol. Chem. 238 (1963) 1141-1144.

4. Zumft, W.G. and Mortenson, L.E. The nitrogen-fixing complex of bacteria. Biochim. Biophys. Acta 416 (1975) 1-52. [PMID: 164247]

5. Adams, M.W.W. The structure and mechanism of iron-hydrogenases. Biochim. Biophys. Acta 1020 (1990) 115-145. [PMID: 2173950]

6. Peters, J.W., Lanzilotta, W.N., Lemon, B.J. and Seefeldt, L.C. X-ray crystal structure of the Fe-only hydrogenase (Cpl) from Clostridium pasteurianum to 1.8 Angstrom resolution. Science 282 (1998) 1853-1858. [PMID: 9836629]

[EC 1.12.7.2 created 1961 as EC 1.98.1.1, transferred 1965 to EC 1.12.1.1, transferred 1972 to EC 1.12.7.1, transferred 1978 to EC 1.18.3.1, transferred 1984 to EC 1.18.99.1, transferred 2002 to EC 1.12.7.2]


EC 1.12.98 With other, known, physiological acceptors

Contents

EC 1.12.98.1 coenzyme F420 hydrogenase
EC 1.12.98.2 5,10-methenyltetrahydromethanopterin hydrogenase
EC 1.12.98.3 Methanosarcina-phenazine hydrogenase

EC 1.12.98.4 sulfhydrogenase
EC 1.12.98.1

Accepted name: coenzyme F420 hydrogenase

Reaction: H2 + oxidized coenzyme F420 = reduced coenzyme F420

For diagram of reaction click here

Glossary: coenzyme F420

Other name(s): 8-hydroxy-5-deazaflavin-reducing hydrogenase; F420-reducing hydrogenase; coenzyme F420-dependent hydrogenase

Systematic name: hydrogen:coenzyme F420 oxidoreductase

Comments: An iron-sulfur flavoprotein (FAD) containing nickel. The enzyme from some sources contains selenocysteine. The enzyme also reduces the riboflavin analogue of F420, flavins and methylviologen, but to a lesser extent. The hydrogen acceptor coenzyme F420 is a deazaflavin derivative.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9027-05-8

References:

1. Adams, M.W.W., Mortenson, L.E. and Chen, J.-S. Hydrogenase. Biochim. Biophys. Acta 594 (1981) 105-176.

2. Yamazaki, S. A selenium-containing hydrogenase from Methanococcus vannielii. Identification of the selenium moiety as a selenocysteine residue. J. Biol. Chem. 257 (1982) 7926-7929. [PMID: 6211447]

3. Fox, J.A., Livingston, D.J., Orme-Johnson, W.H. and Walsh, C.T. 8-Hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum: 1. Purification and characterization. Biochemistry 26 (1987) 4219-4228. [PMID: 3663585]

4. Muth, E., Morschel, E. and Klein, A. Purification and characterization of an 8-hydroxy-5-deazaflavin-reducing hydrogenase from the archaebacterium Methanococcus voltae. Eur. J. Biochem. 169 (1987) 571-577. [PMID: 3121317]

5. Baron, S.F. and Ferry, J.G. Purification and properties of the membrane-associated coenzyme F420-reducing hydrogenase from Methanobacterium formicicum. J. Bacteriol. 171 (1989) 3846-3853. [PMID: 2738024]

[EC 1.12.98.1 created 1989 as EC 1.12.99.1, transferred 2002 to EC 1.12.98.1]

EC 1.12.98.2

Accepted name: 5,10-methenyltetrahydromethanopterin hydrogenase

Reaction: H2 + 5,10-methenyltetrahydromethanopterin = H+ + 5,10-methylenetetrahydromethanopterin

Other name(s): H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase; nonmetal hydrogenase; N5,N10-methenyltetrahydromethanopterin hydrogenase; hydrogen:N5,N10-methenyltetrahydromethanopterin oxidoreductase

Systematic name: hydrogen:5,10-methenyltetrahydromethanopterin oxidoreductase

Comments: Does not catalyse the reduction of artificial dyes. Does not by itself catalyse a H2/H+ exchange reaction. Does not contain nickel or iron-sulfur clusters.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 100357-01-5

References:

1. Zirngibl, C., Hedderich, R. and Thauer, R.K. N5,N10-Methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum has hydrogenase activity. FEBS Lett. 261 (1990) 112-116.

2. Klein, A., Fernandez, V.M. and Thauer, R.K. H2-Forming N5,N10-methylenetetrahydromethanopterin dehydrogenase: mechanism of H2-formation analyzed using hydrogen isotopes. FEBS Lett. 368 (1995) 203-206. [PMID: 7628605]

[EC 1.12.98.2 created 1999 as EC 1.12.99.4, transferred 2002 to EC 1.12.98.2, modified 2004]

EC 1.12.98.3

Accepted name: Methanosarcina-phenazine hydrogenase

Reaction: H2 + 2-(2,3-dihydropentaprenyloxy)phenazine = 2-dihydropentaprenyloxyphenazine

Other name(s): methanophenazine hydrogenase; methylviologen-reducing hydrogenase

Systematic name: hydrogen:2-(2,3-dihydropentaprenyloxy)phenazine oxidoreductase

Comments: Contains nickel, iron-sulfur clusters and cytochrome b. The enzyme from some sources contains selenocysteine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9027-05-8

References:

1. Abken, H.J., Tietze, M., Brodersen, J., Baumer, S., Beifuss, U. and Deppenmeier, U. Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Gö1. J. Bacteriol. 180 (1998) 2027-2032. [PMID: 9555882]

2. Deppenmeier, U., Lienard, T. and Gottschalk, G. Novel reactions involved in energy conservation by methanogenic archaea. FEBS Lett. 457 (1999) 291-297. [PMID: 10471795]

3. Beifuss, U., Tietze, M., Baumer, S. and Deppenmeier, U. Methanophenazine: structure, total synthesis, and function of a new cofactor from methanogenic Archaea. Angew. Chem. Int. Ed. Engl. 39 (2000) 2470-2472. [PMID: 10941105]

[EC 1.12.98.3 created 2002]

EC 1.12.98.4

Accepted name: sulfhydrogenase

Reaction: H2 + (sulfide)n = hydrogen sulfide + (sulfide)n-1

Other name(s): sulfur reductase

Systematic name: H2:polysulfide oxidoreductase

Comments: An iron-sulfur protein. The enzyme from the hyperthermophilic archaeon Pyrococcus furiosus is part of two heterotetrameric complexes where the β and γ subunits function as sulfur reductase and the α and δ subunits function as hydrogenases (EC 1.12.1.3, hydrogen dehydrogenase [NADP+] and EC 1.12.1.4, hydrogen dehydrogenase [NAD(P)+], respectively). Sulfur can also be used as substrate, but since it is insoluble in aqueous solution and polysulfide is generated abiotically by the reaction of hydrogen sulfide and sulfur, polysulfide is believed to be the true substrate [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 101637-43-8

References:

1. Zöphel, A., Kennedy, M.C., Beinert, H. and Kroneck, P.M.H. Investigations on microbial sulfur respiration. 1. Activation and reduction of elemental sulfur in several strains of Eubacteria. Arch. Microbiol. 150 (1988) 72-77.

2. Ma, K., Schicho, R.N., Kelly, R.M. and Adams, M.W. Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: evidence for a sulfur-reducing hydrogenase ancestor. Proc. Natl. Acad. Sci. USA 90 (1993) 5341-5344. [PMID: 8389482]

3. Ma, K., Zhou, Z.H. and Adams, M.W. Hydrogen production from pyruvate by enzymes purified from the hyperthermophilic archaeon, Pyrococcus furiosus: A key role for NADPH. FEMS Microbiol. Lett. 122 (1994) 245-250.

4. Ma, K., Weiss, R. and Adams, M.W. Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction. J. Bacteriol. 182 (2000) 1864-1871. [PMID: 10714990]

[EC 1.12.98.4 created 1992 as EC 1.97.1.3, transferred 2013 to EC 1.12.98.4]


EC 1.12.99 With unknown physiological acceptors

Contents

EC 1.12.99.1 now EC 1.12.98.1
EC 1.12.99.2 deleted
EC 1.12.99.3 now EC 1.12.5.1
EC 1.12.99.4 now EC 1.12.98.2
EC 1.12.99.5 now EC 1.13.11.47
EC 1.12.99.6 hydrogenase (acceptor)


[EC 1.12.99.1 Transferred entry: now EC 1.12.98.1, coenzyme F420 hydrogenase (EC 1.12.99.1 created 1989, deleted 2002)]

[EC 1.12.99.2 Deleted entry: coenzyme-M-7-mercaptoheptanoylthreonine-phosphate-heterodisulfide hydrogenase. Now shown to be two enzymes, EC 1.12.98.3, Methanosarcina-phenazine hydrogenase and EC 1.8.98.1, CoB—CoM heterodisulfide reductase. (EC 1.12.99.2 created 1992, deleted 2002)]

[EC 1.12.99.3 Transferred entry: now EC 1.12.5.1, hydrogen:quinone oxidoreductase (EC 1.12.99.3 created 1999, deleted 2002)]

[EC 1.12.99.4 Transferred entry: now EC 1.12.98.2, N5,N10-methenyltetrahydromethanopterin hydrogenase (EC 1.12.99.4 created 1999, deleted 2002)]

[EC 1.12.99.5 Deleted entry: 3,4-dihydroxyquinoline 2,4-dioxygenase. Identical to EC 1.13.11.47 (EC 1.12.99.5 created 1999, deleted 2001)]

EC 1.12.99.6

Accepted name: hydrogenase (acceptor)

Reaction: H2 + acceptor = reduced acceptor

Other name(s): H2 producing hydrogenase[ambiguous]; hydrogen-lyase[ambiguous]; hydrogenlyase[ambiguous]; uptake hydrogenase[ambiguous]; hydrogen:(acceptor) oxidoreductase

Systematic name: hydrogen:acceptor oxidoreductase

Comments: Uses molecular hydrogen for the reduction of a variety of substances. Contains iron-sulfur clusters. The enzyme from some sources contains nickel.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9027-05-8

References:

1. Shug, A.L., Wilson, P.W., Green, D.E. and Mahler, H.R. The role of molybdenum and flavin in hydrogenase. J. Am. Chem. Soc. 76 (1954) 3355-3356.

2. Adams, M.W.W., Mortenson, L.E. and Chen, J.S. Hydrogenase. Biochim. Biophys. Acta 594 (1981) 105-176.

3. Vignais, P.M., Billoud, B. and Meyer, J. Classification and phylogeny of hydrogenases. FEMS Microbiol. Rev. 25 (2001) 455-501. [PMID: 11524134]

[EC 1.12.99.6 created 2002, modified 2003]


Continued with EC 1.13.11
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