Continued from EC 1.7 and EC 1.8
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 other 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 1.10.99 With other 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 acceptors
EC 1.12.99 With other acceptors
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 1.9.3.2 Transferred entry: now included with EC 1.7.2.1, nitrite reductase (NO-forming) (EC 1.9.3.2 created 1965, deleted 2002)]
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]
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: 37256-52-3
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 1.10.1 With NAD+ or NADP+ as acceptor
EC 1.10.2 With a cytochrome as acceptor
EC 1.10.3 With oxygen as acceptor
EC 1.10.99 With other acceptors
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.
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]
Accepted name: ubiquinol—cytochrome-c reductase
Reaction: QH2 + 2 ferricytochrome c = Q + 2 ferrocytochrome c + 2 H+
Other name(s): 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
Systematic name: ubiquinol:ferricytochrome-c oxidoreductase
Comments: Contains cytochromes b-562, b-566 and c1, and a 2-iron ferredoxin. Depending on the organism and physiological conditions, either two or four protons are extruded 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]
EC 1.10.3.9 photosystem II
EC 1.10.3.10 ubiquinol oxidase (H+-transporting)
EC 1.10.3.11 ubiquinol oxidase
EC 1.10.3.12 menaquinol oxidase (H+-transporting)
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]
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.
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]
Accepted name: o-aminophenol oxidase
Reaction: 2 2-aminophenol + O2 + acceptor = 2-aminophenoxazin-3-one + reduced acceptor + 2 H2O (overall reaction)
(1a) 2 2-aminophenol + O2 = 2 6-iminocyclohexa-2,4-dienone + 2 H2O
(1b) 2 6-iminocyclohexa-2,4-dienone + oxidant = 2-aminophenoxazin-3-one + reduced oxidant (spontaneous)
For diagram click here.
Glossary: 6-iminocyclohexa-2,4-dienone = 1,2-benzoquinone monoimine
isophenoxazine = 2-aminophenoxazin-3-one
Other name(s): isophenoxazine synthase; o-aminophenol:O2 oxidoreductase; 2-aminophenol:O2 oxidoreductase; GriF
Systematic name: 2-aminophenol:oxygen oxidoreductase
Comments: A flavoprotein. While the enzyme from the plant Tecoma stans is activated by Mn2+ [1], that from the bacterium Streptomyces griseus (GriF) requires Cu2+ for maximal activity. Two molecules of the product 6-iminocyclohexa-2,4-dienone spontaneously condense with oxidation to yield 2-aminophenoxazin-3-one [4]. 3-Amino-4-hydroxybenzaldehyde, which has a -CHO group at the para-position with respect to the hydroxy group of 2-aminophenol, was found to be the best substrate for GriF [4].
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. Subba Rao, P.V. 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. Suzuki, H., Furusho, Y., Higashi, T., Ohnishi, Y. and Horinouchi, S. A novel o-aminophenol oxidase responsible for formation of the phenoxazinone chromophore of grixazone. J. Biol. Chem. 281 (2006) 824-833. [PMID: 16282322]
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.
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 1.10.3.7 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)]
Accepted name: photosystem II
Reaction: 2 H2O + 2 plastoquinone + 4 hν = 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]
Accepted name: ubiquinol oxidase (H+-transporting)
Reaction: 2 ubiquinol + O2 + n H+in = 2 ubiquinone + 2 H2O + n H+out
Other name(s): cytochrome bb3 oxidase; cytochrome bo oxidase; cytochrome bd-I oxidase
Systematic name: ubiquinol:O2 oxidoreductase (H+-transporting)
Comments: Contains a dinuclear centre comprising two hemes, or heme and copper. Reduction of O2 on the periplasmic side of the membrane leads to release of protons in the periplasm, generating a transmembrane proton gradient. In addition, the bb3 and bo oxidases, but not the bd oxidase, contribute to the proton gradient by actively pumping protons across the membrane.
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. 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]
3. 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]
4. 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]
Accepted name: ubiquinol oxidase
Reaction: 2 ubiquinol + O2 = 2 ubiquinone + 2 H2O
Other name(s): plant alternative oxidase; cyanide-insensitive oxidase; cytochrome bd-II oxidase
Systematic name: ubiquinol:O2 oxidoreductase (non-electrogenic)
Comments: The enzyme in mitochondria from thermogenic tissues of plants and from certain protists contains a dinuclear iron complex. Cytochrome bd-II from Escherichia coli contains a diheme active site.
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. 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]
4. 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]
Accepted name: menaquinol oxidase (H+-transporting)
Reaction: 2 menaquinol + O2 = 2 menaquinone + 2 H2O
Other name(s): cytochrome aa3-600 oxidase; cytochrome bd oxidase
Systematic name: menaquinol:O2 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]
Accepted name: plastoquinol—plastocyanin reductase
Reaction: plastoquinol + 2 oxidized plastocyanin + 2 H+[side 1] = plastoquinone + 2 reduced plastocyanin + 2 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. Cytochrome c-552 can act as acceptor instead of plastocyanin, but more slowly. In chloroplasts, protons are translocated through the thylakoid membrane from the lumen to the stroma.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
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]
Accepted name: ribosyldihydronicotinamide dehydrogenase (quinone)
Reaction: 1-(β-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone = 1-(β-D-ribofuranosyl)nicotinamide + a hydroquinone
For diagram click here.
Other name(s): NRH:quinone oxidoreductase 2; NQO2; 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 oestrogens 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, PDB, CAS registry number: 667919-86-0
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]
Accepted name: violaxanthin de-epoxidase
Reaction: violaxanthin + 2 L-ascorbate = zeaxanthin + 2 L-dehydroascorbate + 2 H2O (overall reaction)
(1a) violaxanthin + L-ascorbate = antheraxanthin + L-dehydroascorbate + H2O
(1b) antheraxanthin + L-ascorbate = zeaxanthin + L-dehydroascorbate + H2O
For diagram click here.
Glossary: violaxanthin = (3S,3'S,5R,5'R,6S,6'S)-5,5',6,6'-tetrahydro-5,6:5',6'-diepoxy-β,β-carotene-3,3'-diol
antheraxanthin = (3R,3'S,5'R,6'S)-5',6'-dihydro-5',6'-epoxy-β,β-carotene-3,3'-diol
zeaxanthin = (3R,3'R)-β,β-carotene-3,3'-diol
Other name(s): VDE
Systematic name: violaxanthin:ascorbate oxidoreductase
Comments: Along with EC 1.14.13.90, zeaxanthin epoxidase, this enzyme forms part of the xanthophyll (or violaxanthin) cycle for controlling the concentration of zeaxanthin in chloroplasts. It is activated by a low pH of the thylakoid lumen (produced by high light intensity). Zeaxanthin induces the dissipation of excitation energy in the chlorophyll of the light-harvesting protein complex of photosystem II. In higher plants the enzyme reacts with all-trans-diepoxides, such as violaxanthin, and all-trans-monoepoxides, but in the alga Mantoniella squamata, only the diepoxides are good substrates.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 57534-73-3
References:
1. Yamamoto, H.Y. and Higashi, R.M. Violaxanthin de-epoxidase. Lipid composition and substrate specificity. Arch. Biochem. Biophys. 190 (1978) 514-522. [PMID: 102251]
2. Rockholm, D.C. and Yamamoto, H.Y. Violaxanthin de-epoxidase. Plant Physiol. 110 (1996) 697-703. [PMID: 8742341]
3. Bugos, R.C., Hieber, A.D. and Yamamoto, H.Y. Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants. J. Biol. Chem. 273 (1998) 15321-15324. [PMID: 9624110]
4. Kuwabara, T., Hasegawa, M., Kawano, M. and Takaichi, S. Characterization of violaxanthin de-epoxidase purified in the presence of Tween 20: effects of dithiothreitol and pepstatin A. Plant Cell Physiol. 40 (1999) 1119-1126. [PMID: 10635115]
5. Latowski, D., Kruk, J., Burda, K., Skrzynecka-Jaskierm, M., Kostecka-Gugala, A. and Strzalka, K. Kinetics of violaxanthin de-epoxidation by violaxanthin de-epoxidase, a xanthophyll cycle enzyme, is regulated by membrane fluidity in model lipid bilayers. Eur. J. Biochem. 269 (2002) 4656-4665. [PMID: 12230579]
6. Goss, R. Substrate specificity of the violaxanthin de-epoxidase of the primitive green alga Mantoniella squamata (Prasinophyceae). Planta 217 (2003) 801-812. [PMID: 12748855]
7. Latowski, D., Akerlund, H.E. and Strzalka, K. Violaxanthin de-epoxidase, the xanthophyll cycle enzyme, requires lipid inverted hexagonal structures for its activity. Biochemistry 43 (2004) 4417-4420. [PMID: 15078086]
EC 1.11.1 Peroxidases
EC 1.11.2 With H2O2 as acceptor, one oxygen atom of which is incorporated into the product
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]
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.
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 1.11.1.4 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)]
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]
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.
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.
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]
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.
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 homoperoxidase. Science 202 (1978) 1094-1096.
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]
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]
Accepted name: phospholipid-hydroperoxide glutathione peroxidase
Reaction: 2 glutathione + a lipid hydroperoxide = glutathione disulfide + lipid + 2 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 acceptor; 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]
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. Involved in the oxidative degradation of lignin in white rot basidiomycetes.
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.
Accepted name: lignin peroxidase
Reaction: (3,4-dimethoxyphenyl)methanol + H2O2 = 3,4-dimethoxybenzaldehyde + 2 H2O
Glossary: veratryl alcohol = 3,4-dimethoxyphenyl)methanol
Other name(s): diarylpropane oxygenase; ligninase I; diarylpropane peroxidase; LiP; diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving)
Systematic name: 1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol:hydrogen-peroxide oxidoreductase
Comments: A hemoprotein, involved in the oxidative breakdown of lignin by white-rot basidiomycete fungi. The enzyme from Phanerochaete chrysosporium oxidizes typical peroxidase dye substrates at the heme iron, a reaction involving the formation of Compound II (FeIV=O); it also oxidizes (3,4-dimethoxyphenyl)methanol (veratryl alcohol) to the radical cation. The bound veratryl alcohol radical is proposed to bring about the oxidative cleavage of C-C and ether (C-O-C) bonds in lignin model compounds of the diarylpropane and arylpropane-aryl ether type.
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. 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]
5. 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]
6. 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]
7. Khindaria, A., Yamazaki, I. and Aust, S.D. Veratryl alcohol oxidation by lignin peroxidase. Biochemistry 34 (1995) 16860-16869. [PMID: 8527462]
8. 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]
9. 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]
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]
Accepted name: versatile peroxidase
Reaction: (1) Reactive Black 5 + H2O2 = oxidized Reactive Black 5 + 2 H2O
(2) donor + H2O2 = oxidized donor + 2 H2O
Glossary: reactive black 5 = tetrasodium 4-amino-5-hydroxy-3,6(bis(4-(2-(sulfonatooxy)ethylsulfonyl)phenyl)azo)-naphthalene-2,7-disulfonate
Other name(s): VP; hybrid peroxidase; polyvalent peroxidase
Systematic name: reactive-black-5: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. 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-Due̱as, 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]
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]
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]
Accepted name: dye decolorizing peroxidase
Reaction: Reactive Blue 5 + H2O2 = phthalate + 2,2′-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate
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, CAS registry number:
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]
Accepted name: prostamide/prostaglandin F2α 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 F2α = (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 F2α = (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 F2α. 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]
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]
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: hydroperoxy fatty acid:NADPH oxidorductase
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]
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]
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]
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]
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 1.12.1 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
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]
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]
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]
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]
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]
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 1.12.7.1 Transferred entry: now EC 1.18.99.1 hydrogenase (EC 1.12.7.1 created 1972, deleted 1978)]
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 1.12.98.4 sulfhydrogenase
EC 1.12.98.1
Accepted name: coenzyme F420 hydrogenase
Reaction: H2 + 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]
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]
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]
Accepted name: sulfhydrogenase
Reaction: H2 + polysulfiden = H2S + polysulfiden-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 H2S and sulfur, polysulfide is believed to be the true substrate [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
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 1.12.99.2 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)]
Accepted name: hydrogenase (acceptor)
Reaction: H2 + A = AH2
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]