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 1.12 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, 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, 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, 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, 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, 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, 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]
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 group of copper proteins that act also on a variety of substituted catechols, and many of which also catalyse the reaction listed under EC 1.14.18.1 monophenol monooxygenase; this is especially true for the classical tyrosinase.
Links to other databases: BRENDA, EXPASY, KEGG, 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.
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, 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: 2 L-ascorbate + O2 = 2 dehydroascorbate + 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, PDB, CAS registry number: 9029-44-1
References:
1. Stark, G.R. and Dawson, C.R. Ascorbic acid oxidase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.),The Enzymes, 2nd ed., vol. 8,Academic Press, New York, 1963, p. 297-311.
Accepted name: o-aminophenol oxidase
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 (i.e. 1,2-benzoquinone monoimine) 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, 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, 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, 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: plastoquinol—plastocyanin reductase
Reaction: plastoquinol-1 + 2 oxidized plastocyanin = plastoquinone + 2 reduced plastocyanin
Other name(s): plastoquinol/plastocyanin oxidoreductase; cytochrome b6/f complex; cytochrome b6/ complex
Systematic name: plastoquinol:oxidized-plastocyanin oxidoreductase
Comments: A cytochrome f,b6 complex separated from chloroplasts. Also acts, more slowly, on plastoquinol-9 and ubiquinols. Cytochrome c-552 can act instead of plastocyanin, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 79079-13-3
References:
1. Hurt, E. and Hauska, G. A cytochrome f/b6 complex of five polypeptides with plastoquinol-plastocyanin-oxidoreductase activity from spinach chloroplasts. Biochem. J. 117 (1981) 591-595. [PMID: 6269845]
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, 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: (1) violaxanthin + ascorbate = antheraxanthin + dehydroascorbate + H2O
(2) antheraxanthin + ascorbate = zeaxanthin + dehydroascorbate + H2O
For diagram click here.
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, 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]
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, 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, 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, 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, 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. This enzyme can also act as a peroxidase (EC 1.11.1.7 peroxidase) for which several organic substances, especially ethanol, can act as a hydrogen donor. A manganese protein containing MnIII in the resting state, which also belongs here, is often called pseudocatalase. Enzymes from some microorganisms, such as Penicillium simplicissimum, which exhibit both catalase and peroxidase activity, have sometimes been referred to as catalase-peroxidase.
Links to other databases: BRENDA, EXPASY, KEGG, 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.
2. Herbert, D. and Pinsent, J. Crystalline human erythrocyte catalase. Biochem. J. 43 (1948) 203-205.
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 ed., vol. 8, Academic Press, New York, 1963, p. 147-225.
6. Sumner, J.B. and Dounce, A.L. Crystalline catalase. J. Biol. Chem. 121 (1937) 417-424.
7. 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]
Accepted name: peroxidase
Reaction: donor + H2O2 = oxidized donor + 2 H2O
Other name(s): myeloperoxidase; lactoperoxidase; verdoperoxidase; guaiacol peroxidase; thiocyanate peroxidase; eosinophil peroxidase; Japanese radish peroxidase; horseradish peroxidase (HRP); extensin peroxidase; heme peroxidase; MPO; oxyperoxidase; protoheme peroxidase; pyrocatechol peroxidase; scopoletin peroxidase
Systematic name: donor:hydrogen-peroxide oxidoreductase
Comments: A hemoprotein.
Links to other databases: BRENDA, EXPASY, KEGG, 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.
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.
3. Paul, K.G. Peroxidases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 227-274.
4. Tagawa, K., Shin, M. and Okunuki, K. Peroxidases from wheat germ. Nature (Lond.) 183 (1959) 111.
5. Theorell, H. Preparation and properties of crystalline horseradish peroxidase.Ark. Kemi Mineral. Geol. 16A (1943) No.2. 11pp
Accepted name: iodide peroxidase
Reaction: 2 iodide + H2O2 + 2 H+ = diiodine + 2 H2O
Other name(s): iodotyrosine deiodase; iodinase; iodoperoxidase (heme type); thyroid peroxidase; iodide peroxidase-tyrosine iodinase; iodotyrosine deiodinase; monoiodotyrosine deiodinase; thyroperoxidase; tyrosine iodinase
Systematic name: iodide:hydrogen-peroxide oxidoreductase
Comments: A hemoprotein.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9031-28-1
References:
1. Coval, M.L. and Taurog, A. Purification and iodinating activity of hog thyroid peroxidase. J. Biol. Chem. 242 (1967) 5510-5523. [PMID: 12325367]
2. 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]
3 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.
4. Serif, G.S. and Kirkwood, S. Enzyme systems concerned with the synthesis of monoiodotyrosine. II. Further properties of the soluble and mitochondrial systems.J. Biol. Chem. 233 (1958) 109-115.
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, 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 + HCl + H2O2 = RCl + 2 H2O
Other name(s): chloroperoxidase
Systematic name: chloride:hydrogen-peroxide oxidoreductase
Comments: Brings about the chlorination of a range of organic molecules, forming stable C-Cl bonds. Can also act on Br- and I-. Probably a heme-thiolate protein (P-450).
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9055-20-3
References:
1. 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]
2. 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]
3. Theiler, R., Cook, J.C., Hager, L.P. and Siuda, J.F. Halohydrocarbon synthesis by homoperoxidase. Science 202 (1978) 1094-1096.
Accepted name: L-ascorbate peroxidase
Reaction: L-ascorbate + H2O2 = dehydroascorbate + 2 H2O
Other name(s): L-ascorbic acid peroxidase; L-ascorbic acid-specific peroxidase; ascorbate peroxidase; ascorbic acid peroxidase
Systematic name: L-ascorbate:hydrogen-peroxide oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, 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]
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, 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, 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: 1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + 1-(3,4-dimethoxyphenyl)ethane-1,2-diol + H2O
For diagram, click here
Other name(s): diarylpropane oxygenase; ligninase I; diarylpropane peroxidase; LiP; diarylpropane:oxygen,hydrogen-peroxide oxidoreductase; 1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol: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. Brings about the oxidative cleavage of C-C bonds and ether (C-O-C) bonds in a number of lignin model compounds (of the diarylpropane and arylpropane-aryl ether type). The enzyme also oxidizes benzyl alcohols to aldehydes, via an aromatic cation radical [9]. Involved in the oxidative breakdown of lignin in white rot basidiomycetes. Molecular oxygen may be involved in the reaction of substrate radicals under aerobic conditions [3,8].
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 93792-13-3
References:
1. 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]
2. Renganathan, V., Miki, K. and Gold, M.H. Multiple molecular forms of diarylpropane oxygenase, an H2O2-requiring, lignin-degrading enzyme from Phanerochaete chrysosporium. Arch. Biochem. Biophys. 241 (1985) 304-314. [PMID: 4026322]
3. Tien, M. and Kirk, T.T. Lignin-degrading enzyme from Phanerochaete chrysosporium; purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase. Proc. Natl. Acad. Sci. USA 81 (1984) 2280-2284.
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. Tien, M. and Tu, C.P. Cloning and sequencing of a cDNA for a ligninase from Phanerochaete chrysosporium. Nature 326 (1987) 520-523. [PMID: 3561490]
8. Renganathan, V., Miki, K. and Gold, M.H. Role of molecular oxygen in lignin peroxidase reactions. Arch. Biochem. Biophys. 246 (1986) 155-161. [PMID: 3754412]
9. 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]
10. Kirk, T.K. and Farrell, R.L. Enzymatic "combustion": the microbial degradation of lignin. Annu. Rev. Microbiol. 41 (1987) 465-505. [PMID: 3318677]
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, 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, 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-Duè±as, 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]
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
[EC 1.12.1.1 Transferred entry: now EC 1.18.99.1 hydrogenase (EC 1.12.1.1 created 1965, deleted 1972)]
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, 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; hydrogen dehydrogenase (NADP); hydrogenase [ambiguous]
Systematic name: hydrogen:NADP+ oxidoreductase
Comments: An iron-sulfur flavoprotein.
Links to other databases: BRENDA, EXPASY, KEGG, 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]
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, UM-BBD , PDB, 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, 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, UM-BBD, 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. 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]
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, 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, 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, CAS registry number: 9027-05-8
References:
1. Abken, H.J., Tietze, M., Brodersen, J., Baumer, S., Beifuss, U. and Deppenmeier, U. Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Gö1. J. Bacteriol. 180 (1998) 2027-2032. [PMID: 9555882]
2. Deppenmeier, U., Lienard, T. and Gottschalk, G. Novel reactions involved in energy conservation by methanogenic archaea. FEBS Lett. 457 (1999) 291-297. [PMID: 10471795]
3. Beifuss, U., Tietze, M., Baumer, S. and Deppenmeier, U. Methanophenazine: structure, total synthesis, and function of a new cofactor from methanogenic Archaea. Angew. Chem. Int. Ed. Engl. 39 (2000) 2470-2472. [PMID: 10941105]
[EC 1.12.99.2 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, 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]