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 unknown physiological acceptors
EC 1.10 Acting on diphenols and related substances as donors
EC 1.10.1 With NAD+ or NADP+ as acceptor
EC 1.10.2 With a cytochrome as acceptor
EC 1.10.3 With oxygen as acceptor
EC 1.10.5 With a quinone or related compound as acceptor
EC 1.10.99 With unknown physiological acceptors
EC 1.11 Acting on a peroxide as donors
EC 1.11.1 Peroxidases
EC 1.11.2 With H2O2 as acceptor, one oxygen atom of which is incorporated into the product
EC 1.12 Acting on hydrogen as donors
EC 1.12.1 With NAD+ or NADP+ as acceptor
EC 1.12.2 With a cytochrome as acceptor
EC 1.12.5 With a quinone or similar compound as acceptor
EC 1.12.7 With an iron-sulfur protein as acceptor
EC 1.12.98 With other, known, physiological acceptors
EC 1.12.99 With unnown physiological acceptors
[EC 1.9.3.2 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, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, 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:
References:
1. Yates, M.G. and Nason, A. Electron transport systems of the chemoautotroph Ferrobacillus ferrooxidans. II. Purification and properties of a heat-labile iron-cytochrome c reductase. J. Biol. Chem. 241 (1966) 4872-4880. [PMID: 4288725]
[EC 1.9.99.1 Transferred entry: iron—cytochrome-c reductase. Now EC 1.9.98.1, iron—cytochrome-c reductase (EC 1.9.99.1 created 1972, deleted 2014)]
EC 1.10.1 With NAD+ or NADP+ as acceptor
EC 1.10.2 With a cytochrome as acceptor
EC 1.10.3 With oxygen as acceptor
EC 1.10.5 With a quinone or related compound as acceptor
EC 1.10.99 With other acceptors
EC 1.10.1.1
Accepted name: trans-acenaphthene-1,2-diol dehydrogenase
Reaction: (±)-trans-acenaphthene-1,2-diol + 2 NADP+ = acenaphthenequinone + 2 NADPH + 2 H+
Other name(s): trans-1,2-acenaphthenediol dehydrogenase
Systematic name: (±)-trans-acenaphthene-1,2-diol:NADP+ oxidoreductase
Comments: Some preparations also utilize NAD+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 51901-21-4
References:
1. Hopkins, R.P., Drummond, E.C. and Callaghan, P. Dehydrogenation of trans-acenaphthene-1,2-diol by liver cytosol preparations. Biochem. Soc. Trans. 1 (1973) 989-991.
[EC 1.10.2.2 Transferred entry: quinol—cytochrome-c reductase. Now EC 7.1.1.8, quinol—cytochrome-c reductase (EC 1.10.2.2 created 1978, modified 2013, deleted 2018)]
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, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, 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]
Reaction: 4 2-aminophenol + 3 O2 = 2 2-aminophenoxazin-3-one + 6 H2O
For diagram click here.
Glossary: 2-aminophenoxazin-3-one = isophenoxazine
Other name(s): isophenoxazine synthase; o-aminophenol:O2 oxidoreductase; 2-aminophenol:O2 oxidoreductase
Systematic name: 2-aminophenol:oxygen oxidoreductase
Comments: A flavoprotein which catalyses a 6-electron oxidation. The enzyme from the plant Tecoma stans requires Mn2+ and FAD [1] whereas the fungus Pycnoporus coccineus requires Mn2+ and riboflavin 5′-phosphate [2], the bacteria Streptomyces antibioticus requires Cu2+ [4] and the plant Bauhenia monandra does not require any co-factors [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9013-85-8
References:
1. Nair, P.M. and Vaidynathan, C.S. Isophenoxazine synthase. Biochim. Biophys. Acta 81 (1964) 507-516.
2. Nair, P.M. and Vining, L.C. Isophenoxazine synthase apoenzyme from Pycnoporus coccineus. Biochim. Biophys. Acta 96 (1965) 318-327. [PMID: 14298835]
3. Rao, P.V.S. and Vaidyanathan, C.S. Studies on the metabolism of o-aminophenol. Purification and properties of isophenoxazine synthase from Bauhenia monandra. Arch. Biochem. Biophys. 118 (1967) 388-394. [PMID: 4166439]
4. Barry, C.E., 3rd, Nayar, P.G. and Begley, T.P. Phenoxazinone synthase: mechanism for the formation of the phenoxazinone chromophore of actinomycin. Biochemistry 28 (1989) 6323-6333. [PMID: 2477054]
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]
[EC 1.10.3.10 Transferred entry: ubiquinol oxidase (H+-transporting). Now EC 7.1.1.3, ubiquinol oxidase (H+-transporting) (EC 1.10.3.10 created 2011, modified 2014, deleted 2018)]
Accepted name: ubiquinol oxidase (non-electrogenic)
Reaction: 2 ubiquinol + O2 = 2 ubiquinone + 2 H2O
Other name(s): plant alternative oxidase; cyanide-insensitive oxidase; AOX (gene name); ubiquinol oxidase; ubiquinol:O2 oxidoreductase (non-electrogenic)
Systematic name: ubiquinol:oxygen oxidoreductase (non-electrogenic)
Comments: The enzyme, described from the mitochondria of plants and some fungi and protists, is an alternative terminal oxidase that is not sensitive to cyanide inhibition and does not generate a proton motive force. Unlike the electrogenic terminal oxidases that contain hemes (cf. EC 1.10.3.10 and EC 1.10.3.14), this enzyme contains a dinuclear non-heme iron complex. The function of this oxidase is believed to be dissipating excess reducing power, minimizing oxidative stress, and optimizing photosynthesis in response to changing conditions.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Bendall, D.S. and Bonner, W.D. Cyanide-insensitive respiration in plant mitochondria. Plant Physiol. 47 (1971) 236-245. [PMID: 16657603]
2. Siedow, J.N., Umbach, A.L. and Moore, A.L. The active site of the cyanide-resistant oxidase from plant mitochondria contains a binuclear iron center. FEBS Lett. 362 (1995) 10-14. [PMID: 7698344]
3. Berthold, D.A., Andersson, M.E. and Nordlund, P. New insight into the structure and function of the alternative oxidase. Biochim. Biophys. Acta 1460 (2000) 241-254. [PMID: 11106766]
4. Williams, B.A., Elliot, C., Burri, L., Kido, Y., Kita, K., Moore, A.L. and Keeling, P.J. A broad distribution of the alternative oxidase in microsporidian parasites. PLoS Pathog. 6 (2010) e1000761. [PMID: 20169184]
5. Gandin, A., Duffes, C., Day, D.A. and Cousins, A.B. The absence of alternative oxidase AOX1A results in altered response of photosynthetic carbon assimilation to increasing CO2 in Arabidopsis thaliana. Plant Cell Physiol 53 (2012) 1627-1637. [PMID: 22848123]
[EC 1.10.3.12 Transferred entry: menaquinol oxidase (H+-transporting). Now EC 7.1.1.5, menaquinol oxidase (H+-transporting) (EC 1.10.3.12 created 2011, deleted 2018)]
[EC 1.10.3.13 Transferred entry: caldariellaquinol oxidase (H+-transporting). Now EC 7.1.1.4, caldariellaquinol oxidase (H+-transporting) (EC 1.10.3.13 created 2013, deleted 2018)]
[EC 1.10.3.14 Transferred entry: ubiquinol oxidase (electrogenic, non H+-transporting). Now EC 7.1.1.7, ubiquinol oxidase (electrogenic, proton-motive force generating) (EC 1.10.3.14 created 2014, modified 2017, deleted 2018)]
Accepted name: grixazone synthase
Reaction: 2 3-amino-4-hydroxybenzoate + N-acetyl-L-cysteine + 2 O2 = grixazone B + 4 H2O + CO2
For diagram of reaction click here.
Glossary: grixazone B = 8-amino-9-(N-acetyl-L-cystein-S-yl)-7-oxo-7H-phenoxazine-2-carboxylic acid
Other name(s): GriF
Systematic name: 3-amino-4-hydroxybenzoate:N-acetyl-L-cysteine:oxygen oxidoreductase
Comments: A type 3 multi copper protein. The enzyme, isolated from the bacterium Streptomyces griseus, catalyses an 8 electron oxidation. Activation of the enzyme requires a copper chaperone (GriE). It also acts on 3-amino-4-hydroxybenzaldehyde, giving grixazone A. The second aldehyde group is presumably lost as formate. The enzyme also catalyses the reaction of EC 1.10.3.4 o-aminophenol oxidase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Suzuki, H., Ohnishi, Y., Furusho, Y., Sakuda, S. and Horinouchi, S. Novel benzene ring biosynthesis from C3 and C4 primary metabolites by two enzymes. J. Biol. Chem. 281 (2006) 36944-36951. [PMID: 17003031]
2. Le Roes-Hill, M., Goodwin, C. and Burton, S. Phenoxazinone synthase: what’s in a name. Trends Biotechnol 27 (2009) 248-258. [PMID: 19268377]
Accepted name: dihydrophenazinedicarboxylate synthase
Reaction: (1) (1R,6R)-1,4,5,5a,6,9-hexahydrophenazine-1,6-dicarboxylate + O2 = (1R,10aS)-1,4,10,10a-tetrahydrophenazine-1,6-dicarboxylate + H2O2
(2) (1R,10aS)-1,4,10,10a-tetrahydrophenazine-1,6-dicarboxylate + O2 = (5aS)-5,5a-dihydrophenazine-1,6-dicarboxylate + H2O2
(3) (1R,10aS)-1,4,10,10a-tetrahydrophenazine-1-carboxylate + O2 = (10aS)-10,10a-dihydrophenazine-1-carboxylate + H2O2
(4) (1R)-1,4,5,10-tetrahydrophenazine-1-carboxylate + O2 = (10aS)-5,10-dihydrophenazine-1-carboxylate + H2O2
For diagram of reaction click here.
Other name(s): phzG (gene name)
Systematic name: 1,4,5a,6,9,10a-hexahydrophenazine-1,6-dicarboxylate:oxygen oxidoreductase
Comments: Requires FMN. The enzyme, isolated from the bacteria Pseudomonas fluorescens 2-79 and Burkholderia lata 383, is involved in biosynthesis of the reduced forms of phenazine, phenazine-1-carboxylate, and phenazine-1,6-dicarboxylate, where it catalyses multiple reactions.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Xu, N., Ahuja, E.G., Janning, P., Mavrodi, D.V., Thomashow, L.S. and Blankenfeldt, W. Trapped intermediates in crystals of the FMN-dependent oxidase PhzG provide insight into the final steps of phenazine biosynthesis. Acta Crystallogr. D Biol. Crystallogr. 69 (2013) 1403-1413. [PMID: 23897464]
Accepted name: superoxide oxidase
Reaction: 2 O2 + ubiquinol = 2 superoxide + ubiquinone + 2 H+
Other name(s): SOO; CybB; cytochrome b561; superoxide:ubiquinone oxidoreductase
Systematic name: ubiquinol:oxygen oxidoreductase (superoxide-forming)
Comments: This membrane-bound, di-heme containing enzyme, identified in the bacterium Escherichia coli, is responsible for the detoxification of superoxide in the periplasm. In vivo the reaction proceeds in the opposite direction of that shown and produces oxygen. Superoxide production was only observed when the enzyme was incubated in vitro with an excess of ubiquinol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Murakami, H., Kita, K. and Anraku, Y. Cloning of cybB, the gene for cytochrome b561 of Escherichia coli K12. Mol. Gen. Genet. 198 (1984) 1-6. [PMID: 6097799]
2. Murakami, H., Kita, K. and Anraku, Y. Purification and properties of a diheme cytochrome b561 of the Escherichia coli respiratory chain. J. Biol. Chem 261 (1986) 548-551. [PMID: 3510204]
3. Lundgren, C.AK., Sjostrand, D., Biner, O., Bennett, M., Rudling, A., Johansson, A.L., Brzezinski, P., Carlsson, J., von Ballmoos, C. and Hogbom, M. Scavenging of superoxide by a membrane-bound superoxide oxidase. Nat. Chem. Biol. 14 (2018) 788-793. [PMID: 29915379]
Accepted name: ribosyldihydronicotinamide dehydrogenase (quinone)
Reaction: 1-(β-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone = 1-(β-D-ribofuranosyl)nicotinamide + a quinol
For diagram of reaction click here.
Other name(s): NRH:quinone oxidoreductase 2; NQO2; NAD(P)H:quinone oxidoreductase-2 (misleading); QR2; quinone reductase 2; N-ribosyldihydronicotinamide dehydrogenase (quinone); NAD(P)H:quinone oxidoreductase2 (misleading)
Systematic name: 1-(β-D-ribofuranosyl)-1,4-dihydronicotinamide:quinone oxidoreductase
Comments: A flavoprotein. Unlike EC 1.6.5.2, NAD(P)H dehydrogenase (quinone), this quinone reductase cannot use NADH or NADPH; instead it uses N-ribosyl- and N-alkyldihydronicotinamides. Polycyclic aromatic hydrocarbons, such as benz[a]anthracene, and the estrogens 17β-estradiol and diethylstilbestrol are potent inhibitors, but dicoumarol is only a very weak inhibitor [2]. This enzyme can catalyse both 2-electron and 4-electron reductions, but one-electron acceptors, such as potassium ferricyanide, cannot be reduced [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Liao, S., Dulaney, J.T. and Williams-Ashman, H.G. Purification and properties of a flavoprotein catalyzing the oxidation of reduced ribosyl nicotinamide. J. Biol. Chem. 237 (1962) 2981-2987. [PMID: 14465018]
2. Zhao, Q., Yang, X.L., Holtzclaw, W.D. and Talalay, P. Unexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase). Proc. Natl. Acad. Sci. USA 94 (1997) 1669-1674. [PMID: 9050836]
3. Wu, K., Knox, R., Sun, X.Z., Joseph, P., Jaiswal, A.K., Zhang, D., Deng, P.S. and Chen, S. Catalytic properties of NAD(P)H:quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase. Arch. Biochem. Biophys. 347 (1997) 221-228. [PMID: 9367528]
4. Jaiswal, A.K. Human NAD(P)H:quinone oxidoreductase2. Gene structure, activity, and tissue-specific expression. J. Biol. Chem. 269 (1994) 14502-14508. [PMID: 8182056]
[EC 1.10.9.1 Transferred entry: plastoquinol—plastocyanin reductase. Now EC 7.1.1.6, plastoquinol—plastocyanin reductase (EC 1.10.9.1 created 1984 as EC 1.10.99.1, transferred 2011 to EC 1.10.9.1, deleted 2018)]
[EC 1.10.99.2 Transferred entry: ribosyldihydronicotinamide dehydrogenase (quinone). Now classified as EC 1.10.5.1, ribosyldihydronicotinamide dehydrogenase (quinone). (EC 1.10.99.2 created 2005, deleted 2014)]
[EC 1.10.99.3 Transferred entry: violaxanthin de-epoxidase. Now classified as EC 1.23.5.1, violaxanthin de-epoxidase. (EC 1.10.99.3 created 2005, deleted 2014)]
EC 1.11.1 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, PDB, 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, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, 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; iodoperoxidase (heme type); iodide peroxidase-tyrosine iodinase; thyroperoxidase; tyrosine iodinase; TPO; iodinase
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, PDB, 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 bromoperoxidase. Science 202 (1978) 1094-1096. [PMID: 17777960]
4. Sundaramoorthy, M., Terner, J. and Poulos, T.L. The crystal structure of chloroperoxidase: a heme peroxidase—cytochrome P450 functional hybrid. Structure 3 (1995) 1367-1377. [PMID: 8747463]
5. ten Brink, H.B., Tuynman, A., Dekker, H.L., Hemrika, W., Izumi, Y., Oshiro, T., Schoemaker, H.E. and Wever, R. Enantioselective sulfoxidation catalyzed by vanadium haloperoxidases. Inorg. Chem. 37 (1998) 6780-6784. [PMID: 11670813]
6. ten Brink, H.B., Dekker, H.L., Schoemaker, H.E. and Wever, R. Oxidation reactions catalyzed by vanadium chloroperoxidase from Curvularia inaequalis. J. Inorg. Biochem. 80 (2000) 91-98. [PMID: 10885468]
7. Manoj, K.M. Chlorinations catalyzed by chloroperoxidase occur via diffusible intermediate(s) and the reaction components play multiple roles in the overall process. Biochim. Biophys. Acta 1764 (2006) 1325-1339. [PMID: 16870515]
8. Kuhnel, K., Blankenfeldt, W., Terner, J. and Schlichting, I. Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate. J. Biol. Chem. 281 (2006) 23990-23998. [PMID: 16790441]
9. Manoj, K.M. and Hager, L.P. Chloroperoxidase, a janus enzyme. Biochemistry 47 (2008) 2997-3003. [PMID: 18220360]
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 hydroperoxy-fatty-acyl-[lipid] = glutathione disulfide + a hydroxy-fatty-acyl-[lipid] + H2O
Other name(s): peroxidation-inhibiting protein; PHGPX; peroxidation-inhibiting protein:peroxidase,glutathione (phospholipid hydroperoxide-reducing); phospholipid hydroperoxide glutathione peroxidase; hydroperoxide glutathione peroxidase
Systematic name: glutathione:lipid-hydroperoxide oxidoreductase
Comments: A protein containing a selenocysteine residue. The products of action of EC 1.13.11.12 lipoxygenase on phospholipids can act as acceptors; H2O2 can also act, but much more slowly (cf. EC 1.11.1.9 glutathione peroxidase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 97089-70-8
References:
1. Ursini, F., Maiorino, M. and Gregolin, C. The selenoenzyme phospholipid hydroperoxide glutathione peroxidase. Biochim. Biophys. Acta 839 (1985) 62-70. [PMID: 3978121]
2. Schnurr, K., Belkner, J., Ursini, F., Schewe, T. and Kuhn, H. The selenoenzyme phospholipid hydroperoxide glutathione peroxidase controls the activity of the 15-lipoxygenase with complex substrates and preserves the specificity of the oxygenation products. J. Biol. Chem. 271 (1996) 4653-4658. [PMID: 8617728]
Accepted name: manganese peroxidase
Reaction: 2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
Other name(s): peroxidase-M2; Mn-dependent (NADH-oxidizing) peroxidase
Systematic name: Mn(II):hydrogen-peroxide oxidoreductase
Comments: A hemoprotein. The enzyme from white rot basidiomycetes is involved in the oxidative degradation of lignin. The enzyme oxidizes a bound Mn2+ ion to Mn3+ in the presence of hydrogen peroxide. The product, Mn3+, is released from the active site in the presence of a chelator (mostly oxalate and malate) that stabilizes it against disproportionation to Mn2+ and insoluble Mn4+ [4]. The complexed Mn3+ ion can diffuse into the lignified cell wall, where it oxidizes phenolic components of lignin and other organic substrates [1]. It is inactive with veratryl alcohol or nonphenolic substrates.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 114995-15-2
References:
1. Glenn, J.K., Akileswaran, L. and Gold, M.H. Mn(II) oxidation is the principal function of the extracellular Mn-peroxidase from Phanerochaete chrysosporium. Arch. Biochem. Biophys. 251 (1986) 688-696.
2. Paszczynski, A., Huynh, V.-B. and Crawford, R. Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium. Arch. Biochem. Biophys. 244 (1986) 750-765. [PMID: 3080953]
3. Wariishi, H., Akileswaran, L. and Gold, M.H. Manganese peroxidase from the basidiomycete Phanerochaete chrysosporium: spectral characterization of the oxidized states and the catalytic cycle. Biochemistry 27 (1988) 5365-5370.
4. Kuan, I.C. and Tien, M. Stimulation of Mn peroxidase activity: a possible role for oxalate in lignin biodegradation. Proc. Natl. Acad. Sci. USA 90 (1993) 1242-1246. [PMID: 8433984]
Accepted name: lignin peroxidase
Reaction: (1) 1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O
(2) 2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O
Glossary: veratryl alcohol = (3,4-dimethoxyphenyl)methanol
veratraldehyde = 3,4-dimethoxybenzaldehyde
2-methoxyphenol = guaiacol
Other name(s): diarylpropane oxygenase; ligninase I; diarylpropane peroxidase; LiP; diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving); 1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol:hydrogen-peroxide oxidoreductase (incorrect); (3,4-dimethoxyphenyl)methanol:hydrogen-peroxide oxidoreductase
Systematic name: 1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol:hydrogen-peroxide oxidoreductase
Comments: A hemoprotein, involved in the oxidative breakdown of lignin by white-rot basidiomycete fungi. The reaction involves an initial oxidation of the heme iron by hydrogen peroxide, forming compound I (FeIV=O radical cation) at the active site. A single one-electron reduction of compound I by an electron derived from a substrate molecule yields compound II (FeIV=O non-radical cation), followed by a second one-electron transfer that returns the enzyme to the ferric oxidation state. The electron transfer events convert the substrate molecule into a transient cation radical intermediate that fragments spontaneously. The enzyme can act on a wide range of aromatic compounds, including methoxybenzenes and nonphenolic β-O-4 linked arylglycerol β-aryl ethers, but cannot act directly on the lignin molecule, which is too large to fit into the active site. However larger lignin molecules can be degraded in the presence of veratryl alcohol. It has been suggested that the free radical that is formed when the enzyme acts on veratryl alcohol can diffuse into the lignified cell wall, where it oxidizes lignin and other organic substrates. In the presence of high concentration of hydrogen peroxide and lack of substrate, the enzyme forms a catalytically inactive form (compound III). This form can be rescued by interaction with two molecules of the free radical products. In the case of veratryl alcohol, such an interaction yields two molecules of veratryl aldehyde.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 93792-13-3
References:
1. Kersten, P.J., Tien, M., Kalyanaraman, B. and Kirk, T.K. The ligninase of Phanerochaete chrysosporium generates cation radicals from methoxybenzenes. J. Biol. Chem. 260 (1985) 2609-2612. [PMID: 2982828]
2. Paszczynski, A., Huynh, V.-B. and Crawford, R. Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium, Arch. Biochem. Biophys. 244 (1986) 750-765. [PMID: 3080953]
3. Harvey, P.J., Schoemaker, H.E. and Palmer, J.M. Veratryl alcohol as a mediator and the role of radical cations in lignin biodegradation by Phanerochaete chrysosporium, FEBS Lett. 195 (1986) 242-246.
4. Wariishi, H., Marquez, L., Dunford, H.B. and Gold, M.H. Lignin peroxidase compounds II and III. Spectral and kinetic characterization of reactions with peroxides. J. Biol. Chem. 265 (1990) 11137-11142. [PMID: 2162833]
5. Cai, D.Y. and Tien, M. Characterization of the oxycomplex of lignin peroxidases from Phanerochaete chrysosporium: equilibrium and kinetics studies. Biochemistry 29 (1990) 2085-2091. [PMID: 2328240]
6. Khindaria, A., Yamazaki, I. and Aust, S.D. Veratryl alcohol oxidation by lignin peroxidase. Biochemistry 34 (1995) 16860-16869. [PMID: 8527462]
7. Khindaria, A., Yamazaki, I. and Aust, S.D. Stabilization of the veratryl alcohol cation radical by lignin peroxidase. Biochemistry 35 (1996) 6418-6424. [PMID: 8639588]
8. Khindaria, A., Nie, G. and Aust, S.D. Detection and characterization of the lignin peroxidase compound II-veratryl alcohol cation radical complex. Biochemistry 36 (1997) 14181-14185. [PMID: 9369491]
9. Doyle, W.A., Blodig, W., Veitch, N.C., Piontek, K. and Smith, A.T. Two substrate interaction sites in lignin peroxidase revealed by site-directed mutagenesis. Biochemistry 37 (1998) 15097-15105. [PMID: 9790672]
10. Pollegioni, L., Tonin, F. and Rosini, E. Lignin-degrading enzymes. FEBS J. 282 (2015) 1190-1213. [PMID: 25649492]
[EC 1.11.1.15 Transferred entry: peroxiredoxin. Now described by EC 1.11.1.24, thioredoxin-dependent peroxiredoxin; EC 1.11.1.25, glutaredoxin-dependent peroxiredoxin; EC 1.11.1.26, NADH-dependent peroxiredoxin; EC 1.11.1.27, glutathione-dependent peroxiredoxin; EC 1.11.1.28, lipoyl-dependent peroxiredoxin; and EC 1.11.1.29, mycoredoxin-dependent peroxiredoxin. (EC 1.11.1.15 created 2004, deleted 2019)]
Accepted name: versatile peroxidase
Reaction: (1) 1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O
(2) 2 manganese(II) + 2 H+ + H2O2 = 2 manganese(III) + 2 H2O
Glossary: 4-hydroxy-3-methoxybenzaldehyde = vanillin
2-methoxyphenol = guaiacol
Other name(s): VP; hybrid peroxidase; polyvalent peroxidase; reactive-black-5:hydrogen-peroxide oxidoreductase
Systematic name: 1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol:hydrogen-peroxide oxidoreductase
Comments: A hemoprotein. This ligninolytic peroxidase combines the substrate-specificity characteristics of the two other ligninolytic peroxidases, EC 1.11.1.13, manganese peroxidase and EC 1.11.1.14, lignin peroxidase. Unlike these two enzymes, it is also able to oxidize phenols, hydroquinones and both low- and high-redox-potential dyes, due to a hybrid molecular architecture that involves multiple binding sites for substrates [2,4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 42613-30-9, 114995-15-2
References:
1. Martínez, M.J., Ruiz-Dueñas, F.J., Guillén, F. and Martínez, A.T. Purification and catalytic properties of two manganese peroxidase isoenzymes from Pleurotus eryngii, Eur. J. Biochem. 237 (1996) 424-432. [PMID: 8647081]
2. Heinfling, A., Ruiz-Dueñas, F.J., Martínez, M.J., Bergbauer, M., Szewzyk, U. and Martínez, A.T. A study on reducing substrates of manganese-oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta, FEBS Lett. 428 (1998) 141-146. [PMID: 9654123]
3. Ruiz-Dueñas, F.J., Martínez, M.J. and Martínez, A.T. Molecular characterization of a novel peroxidase isolated from the ligninolytic fungus Pleurotus eryngii, Mol. Microbiol. 31 (1999) 223-235. [PMID: 9987124]
4. Camarero, S., Sarkar, S., Ruiz-Dueñas, F.J., Martínez, M.J. and Martínez, A.T. Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites. J. Biol. Chem. 274 (1999) 10324-10330. [PMID: 10187820]
5. Ruiz-Dueñas, F.J., Martínez, M.J. and Martínez, A.T. Heterologous expression of Pleurotus eryngii peroxidase confirms its ability to oxidize Mn2+ and different aromatic substrates. Appl. Environ. Microbiol. 65 (1999) 4705-4707. [PMID: 10508113]
6. Camarero, S., Ruiz-Dueñas, F.J., Sarkar, S., Martínez, M.J. and Martínez, A.T. The cloning of a new peroxidase found in lignocellulose cultures of Pleurotus eryngii and sequence comparison with other fungal peroxidases. FEMS Microbiol. Lett. 191 (2000) 37-43. [PMID: 11004397]
7. Ruiz-Dueñas, F.J., Camarero, S., Pérez-Boada, M., Martínez, M.J. and Martínez, A.T. A new versatile peroxidase from Pleurotus, Biochem. Soc. Trans. 29 (2001) 116-122. [PMID: 11356138]
8. Banci, L., Camarero, S., Martínez, A.T., Martínez, M.J., Pérez-Boada, M., Pierattelli, R. and Ruiz-Dueñas, F.J. NMR study of manganese(II) binding by a new versatile peroxidase from the white-rot fungus Pleurotus eryngii, J. Biol. Inorg. Chem. 8 (2003) 751-760. [PMID: 12884090]
9. Pérez-Boada, M., Ruiz-Dueñas, F.J., Pogni, R., Basosi, R., Choinowski, T., Martínez, M.J., Piontek, K. and Martínez, A.T. Versatile peroxidase oxidation of high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and crystallographic investigation of three long-range electron transfer pathways. J. Mol. Biol. 354 (2005) 385-402. [PMID: 16246366]
10. Caramelo, L., Martínez, M.J. and Martínez, A.T. A search for ligninolytic peroxidases in the fungus Pleurotus eryngii involving α-keto-γ-thiomethylbutyric acid and lignin model dimer. Appl. Environ. Microbiol. 65 (1999) 916-922. [PMID: 10049842]
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 + 2 H2O2 = phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O
Glossary: Reactive Blue 5 = 1-amino-4-{[3-({4-chloro-6-[(3-sulfophenyl)amino]-1,3,5-triazin-2-yl}amino)-4-sulfophenyl]amino}-9,10-dihydro-9,10-dioxoanthracene-2-sulfonic acid
Other name(s): DyP; DyP-type peroxidase
Systematic name: Reactive-Blue-5:hydrogen-peroxide oxidoreductase
Comments: Heme proteins with proximal histidine secreted by basidiomycetous fungi and eubacteria. They are similar to EC 1.11.1.16 versatile peroxidase (oxidation of Reactive Black 5, phenols, veratryl alcohol), but differ from the latter in their ability to efficiently oxidize a number of recalcitrant anthraquinone dyes, and inability to oxidize Mn(II). The model substrate Reactive Blue 5 is converted with high efficiency via a so far unique mechanism that combines oxidative and hydrolytic steps and leads to the formation of phthalic acid. Bacterial TfuDyP catalyses sulfoxidation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc PDB, 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: NADPH:hydroperoxy fatty acid oxidoreductase
Comments: The enzyme, characterized from the cyanobacterium Synechocystis PCC 6803, can reduce unsaturated fatty acid hydroperoxides and alkyl hydroperoxides. The enzyme, which utilizes NADPH generated by the photosynthetic electron transfer system, protects the cells from lipid peroxidation.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Gaber, A., Tamoi, M., Takeda, T., Nakano, Y. and Shigeoka, S. NADPH-dependent glutathione peroxidase-like proteins (Gpx-1, Gpx-2) reduce unsaturated fatty acid hydroperoxides in Synechocystis PCC 6803. FEBS Lett 499 (2001) 32-36. [PMID: 11418106]
2. Gaber, A., Yoshimura, K., Tamoi, M., Takeda, T., Nakano, Y. and Shigeoka, S. Induction and functional analysis of two reduced nicotinamide adenine dinucleotide phosphate-dependent glutathione peroxidase-like proteins in Synechocystis PCC 6803 during the progression of oxidative stress. Plant Physiol. 136 (2004) 2855-2861. [PMID: 15347790]
Accepted name: (S)-2-hydroxypropylphosphonic acid epoxidase
Reaction: (S)-2-hydroxypropylphosphonate + H2O2 = (1R,2S)-1,2-epoxypropylphosphonate + 2 H2O
For diagram of reaction click here.
Glossary: (1R,2S)-1,2-epoxypropylphosphonate = fosfomycin = [(2R,3S)-3-methyloxiran-2-yl]phosphonate
Other name(s): HPP epoxidase; HppE; 2-hydroxypropylphosphonic acid epoxidase; Fom4; (S)-2-hydroxypropylphosphonate epoxidase
Systematic name: (S)-2-hydroxypropylphosphonate:hydrogen-peroxide epoxidase
Comments: This is the last enzyme in the biosynthetic pathway of fosfomycin, a broad-spectrum antibiotic produced by certain Streptomyces species. Contains non heme iron that forms a iron(IV)-oxo (ferryl) complex with hydrogen peroxide, which functions as a proton abstractor from the substrate [7].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Munos, J.W., Moon, S.J., Mansoorabadi, S.O., Chang, W., Hong, L., Yan, F., Liu, A. and Liu, H.W. Purification and characterization of the epoxidase catalyzing the formation of fosfomycin from Pseudomonas syringae. Biochemistry 47 (2008) 8726-8735. [PMID: 18656958]
2. Yan, F., Moon, S.J., Liu, P., Zhao, Z., Lipscomb, J.D., Liu, A. and Liu, H.W. Determination of the substrate binding mode to the active site iron of (S)-2-hydroxypropylphosphonic acid epoxidase using 17O-enriched substrates and substrate analogues. Biochemistry 46 (2007) 12628-12638. [PMID: 17927218]
3. Hidaka, T., Goda, M., Kuzuyama, T., Takei, N., Hidaka, M. and Seto, H. Cloning and nucleotide sequence of fosfomycin biosynthetic genes of Streptomyces wedmorensis. Mol. Gen. Genet. 249 (1995) 274-280. [PMID: 7500951]
4. Liu, P., Mehn, M.P., Yan, F., Zhao, Z., Que, L., Jr. and Liu, H.W. Oxygenase activity in the self-hydroxylation of (S)-2-hydroxypropylphosphonic acid epoxidase involved in fosfomycin biosynthesis. J. Am. Chem. Soc. 126 (2004) 10306-10312. [PMID: 15315444]
5. Higgins, L.J., Yan, F., Liu, P., Liu, H.W. and Drennan, C.L. Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme. Nature 437 (2005) 838-844. [PMID: 16015285]
6. Cameron, S., McLuskey, K., Chamberlayne, R., Hallyburton, I. and Hunter, W.N. Initiating a crystallographic analysis of recombinant (S)-2-hydroxypropylphosphonic acid epoxidase from Streptomyces wedmorensis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 (2005) 534-536. [PMID: 16511089]
7. Wang, C., Chang, W.C., Guo, Y., Huang, H., Peck, S.C., Pandelia, M.E., Lin, G.M., Liu, H.W., Krebs, C. and Bollinger, J.M., Jr. Evidence that the fosfomycin-producing epoxidase, HppE, is a non-heme-iron peroxidase. Science 342 (2013) 991-995. [PMID: 24114783]
Accepted name: thioredoxin-dependent peroxiredoxin
Reaction: thioredoxin + ROOH = thioredoxin disulfide + H2O + ROH
For diagram of reaction, click here and for mechanism, click here
Other name(s): thioredoxin peroxidase; bcp (gene name); tpx (gene name); PrxQ
Systematic name: thioredoxin: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 [4]. 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 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. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Thioredoxin-dependent peroxiredoxins are the most common. They have been reported from archaea, bacteria, fungi, plants, and animals.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Kang, S.W., Chae, H.Z., Seo, M.S., Kim, K., Baines, I.C. and Rhee, S.G. Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-α. J. Biol. Chem. 273 (1998) 6297-6302. [PMID: 9497357]
2. Kong, W., Shiota, S., Shi, Y., Nakayama, H. and Nakayama, K. A novel peroxiredoxin of the plant Sedum lineare is a homologue of Escherichia coli bacterioferritin co-migratory protein (Bcp). Biochem. J. 351 (2000) 107-114. [PMID: 10998352]
3. Jeong, W., Cha, M.K. and Kim, I.H. Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin comigratory protein (BCP) as a new member of the thiol-specific antioxidant protein (TSA)/alkyl hydroperoxide peroxidase C (AhpC) family. J. Biol. Chem. 275 (2000) 2924-2930. [PMID: 10644761]
4. 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]
5. Jeon, S.J. and Ishikawa, K. Characterization of novel hexadecameric thioredoxin peroxidase from Aeropyrum pernix K1. J. Biol. Chem. 278 (2003) 24174-24180. [PMID: 12707274]
6. Perez-Perez, M.E., Mata-Cabana, A., Sanchez-Riego, A.M., Lindahl, M. and Florencio, F.J. A comprehensive analysis of the peroxiredoxin reduction system in the cyanobacterium Synechocystis sp. strain PCC 6803 reveals that all five peroxiredoxins are thioredoxin dependent. J. Bacteriol. 191 (2009) 7477-7489. [PMID: 19820102]
Accepted name: glutaredoxin-dependent peroxiredoxin
Reaction: glutaredoxin + ROOH = glutaredoxin disulfide + H2O + ROH
For diagram of reaction, click here and for mechanism, click here
Other name(s): PRXIIB (gene name)
Systematic name: glutaredoxin: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 [2]. 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 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. To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Glutaredoxin-dependent peroxiredoxins have been reported from bacteria, fungi, plants, and animals. These enzymes are often able to use an alternative reductant such as thioredoxin or glutathione.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Rouhier, N., Gelhaye, E. and Jacquot, J.P. Glutaredoxin-dependent peroxiredoxin from poplar: protein-protein interaction and catalytic mechanism. J. Biol. Chem. 277 (2002) 13609-13614. [PMID: 11832487]
2. 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]
3. Pedrajas, J.R., Padilla, C.A., McDonagh, B. and Barcena, J.A. Glutaredoxin participates in the reduction of peroxides by the mitochondrial 1-CYS peroxiredoxin in Saccharomyces cerevisiae. Antioxid Redox Signal 13 (2010) 249-258. [PMID: 20059400]
4. Hanschmann, E.M., Lonn, M.E., Schutte, L.D., Funke, M., Godoy, J.R., Eitner, S., Hudemann, C. and Lillig, C.H. Both thioredoxin 2 and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-Cys peroxiredoxin Prx3. J. Biol. Chem. 285 (2010) 40699-40705. [PMID: 20929858]
5. Lim, J.G., Bang, Y.J. and Choi, S.H. Characterization of the Vibrio vulnificus 1-Cys peroxiredoxin Prx3 and regulation of its expression by the Fe-S cluster regulator IscR in response to oxidative stress and iron starvation. J. Biol. Chem. 289 (2014) 36263-36274. [PMID: 25398878]
6. Couturier, J., Prosper, P., Winger, A.M., Hecker, A., Hirasawa, M., Knaff, D.B., Gans, P., Jacquot, J.P., Navaza, A., Haouz, A. and Rouhier, N. In the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima. Antioxid Redox Signal 18 (2013) 1613-1622. [PMID: 22866991]
Accepted name: NADH-dependent peroxiredoxin
Reaction: NADH + ROOH + H+ = NAD+ + H2O + ROH
For diagram of reaction, click here and for mechanism, click here
Other name(s): ahpC (gene name); ahpF (gene name); alkyl hydroperoxide reductase
Systematic name: NADH: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 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. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. This bacterial peroxiredoxin differs from most other forms by comprising two types of subunits. One subunit (AhpC) is a typical 2-Cys peroxiredoxin. Following the reduction of the substrate, one AhpC subunit forms a disulfide bond with an identical unit. The disulfide bond is reduced by the second type of subunit (AhpF). This second subunit is a flavin-containing protein that uses electrons from NADH to reduce the cysteine residues on the AhpC subunits back to their active state.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
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. Dip, P.V., Kamariah, N., Subramanian Manimekalai, M.S., Nartey, W., Balakrishna, A.M., Eisenhaber, F., Eisenhaber, B. and Gruber, G. Structure, mechanism and ensemble formation of the alkylhydroperoxide reductase subunits AhpC and AhpF from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 70 (2014) 2848-2862. [PMID: 25372677]
3. Nartey, W., Basak, S., Kamariah, N., Manimekalai, M.S., Robson, S., Wagner, G., Eisenhaber, B., Eisenhaber, F. and Gruber, G. NMR studies reveal a novel grab and release mechanism for efficient catalysis of the bacterial 2-Cys peroxiredoxin machinery. FEBS J. 282 (2015) 4620-4638. [PMID: 26402142]
Accepted name: glutathione-dependent peroxiredoxin
Reaction: glutathione + ROOH = glutathione disulfide + H2O + ROH
For diagram of reaction, click here and for mechanism, click here
Other name(s): PRDX6 (gene name); prx3 (gene name)
Systematic name: glutathione: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 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. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Glutathione-dependent peroxiredoxins have been reported from bacteria and animals, and appear to be 1-Cys enzymes. The mechanism for the mammalian PRDX6 enzyme involves heterodimerization of the enzyme with π-glutathione S-transferase, followed by glutathionylation of the oxidized cysteine residue. Subsequent dissociation of the heterodimer yields glutathionylated peroxiredoxin, which is restored to the active form via spontaneous reduction by a second glutathione molecule.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
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. Pauwels, F., Vergauwen, B., Vanrobaeys, F., Devreese, B. and Van Beeumen, J.J. Purification and characterization of a chimeric enzyme from Haemophilus influenzae Rd that exhibits glutathione-dependent peroxidase activity. J. Biol. Chem. 278 (2003) 16658-16666. [PMID: 12606554]
3. Manevich, Y., Feinstein, S.I. and Fisher, A.B. Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with π GST. Proc. Natl. Acad. Sci. USA 101 (2004) 3780-3785. [PMID: 15004285]
4. Greetham, D. and Grant, C.M. Antioxidant activity of the yeast mitochondrial one-Cys peroxiredoxin is dependent on thioredoxin reductase and glutathione in vivo. Mol. Cell Biol. 29 (2009) 3229-3240. [PMID: 19332553]
5. Lim, J.G., Bang, Y.J. and Choi, S.H. Characterization of the Vibrio vulnificus 1-Cys peroxiredoxin Prx3 and regulation of its expression by the Fe-S cluster regulator IscR in response to oxidative stress and iron starvation. J. Biol. Chem. 289 (2014) 36263-36274. [PMID: 25398878]
Accepted name: lipoyl-dependent peroxiredoxin
Reaction: a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + ROOH = a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + ROH
For diagram of reaction, click here and for mechanism, click here
Other name(s): Ohr; ahpC (gene name); ahpD (gene name)
Systematic name: lipoyl: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 [2]. 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 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. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Two types of lipoyl-dependent peroxiredoxins have been reported from bacteria. One type is the AhpC/AhpD system, originally described from Mycobacterium tuberculosis. In that system, AhpC catalyses reduction of the substrate, resulting in an intramolecular disulfide. AhpD then forms an intermolecular disulfide crosslink with AhpC, reducing it back to active state. AhpD is reduced in turn by lipoylated proteins. The second type, which has been characterized in Xylella fastidiosa, consists of only one type of subunit, which interacts directly with lipoylated proteins.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Hillas, P.J., del Alba, F.S., Oyarzabal, J., Wilks, A. and Ortiz De Montellano, P.R. The AhpC and AhpD antioxidant defense system of Mycobacterium tuberculosis. J. Biol. Chem. 275 (2000) 18801-18809. [PMID: 10766746]
2. 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]
3. Koshkin, A., Nunn, C.M., Djordjevic, S. and Ortiz de Montellano, P.R. The mechanism of Mycobacterium tuberculosis alkylhydroperoxidase AhpD as defined by mutagenesis, crystallography, and kinetics. J. Biol. Chem. 278 (2003) 29502-29508. [PMID: 12761216]
4. Koshkin, A., Knudsen, G.M. and Ortiz De Montellano, P.R. Intermolecular interactions in the AhpC/AhpD antioxidant defense system of Mycobacterium tuberculosis. Arch. Biochem. Biophys. 427 (2004) 41-47. [PMID: 15178486]
5. Shi, S. and Ehrt, S. Dihydrolipoamide acyltransferase is critical for Mycobacterium tuberculosis pathogenesis. Infect. Immun. 74 (2006) 56-63. [PMID: 16368957]
6. Cussiol, J.R., Alegria, T.G., Szweda, L.I. and Netto, L.E. Ohr (organic hydroperoxide resistance protein) possesses a previously undescribed activity, lipoyl-dependent peroxidase. J. Biol. Chem. 285 (2010) 21943-21950. [PMID: 20463026]
Accepted name: mycoredoxin-dependent peroxiredoxin
Reaction: mycoredoxin + ROOH = mycoredoxin disulfide + H2O + ROH
For diagram of reaction, click here and for mechanism, click here
Other name(s): ahpE (gene name)
Systematic name: mycoredoxin: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 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. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Mycoredoxin-dependent enzymes are found in Mycobacteria. Following the reduction of the substrate, the sulfenic acid derivative of the peroxidatic cysteine forms a protein mixed disulfide with the N-terminal cysteine of mycoredoxin, which is then reduced by the C-terminal cysteine of mycoredoxin, restoring the peroxiredoxin to active state and resulting in an intra-protein disulfide in mycoredoxin. The disulfide is eventually reduced by mycothiol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
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. Hugo, M., Turell, L., Manta, B., Botti, H., Monteiro, G., Netto, L.E., Alvarez, B., Radi, R. and Trujillo, M. Thiol and sulfenic acid oxidation of AhpE, the one-cysteine peroxiredoxin from Mycobacterium tuberculosis: kinetics, acidity constants, and conformational dynamics. Biochemistry 48 (2009) 9416-9426. [PMID: 19737009]
3. Hugo, M., Van Laer, K., Reyes, A.M., Vertommen, D., Messens, J., Radi, R. and Trujillo, M. Mycothiol/mycoredoxin 1-dependent reduction of the peroxiredoxin AhpE from Mycobacterium tuberculosis. J. Biol. Chem. 289 (2014) 5228-5239. [PMID: 24379404]
4. Kumar, A., Balakrishna, A.M., Nartey, W., Manimekalai, M.SS. and Gruber, G. Redox chemistry of Mycobacterium tuberculosis alkylhydroperoxide reductase E (AhpE): Structural and mechanistic insight into a mycoredoxin-1 independent reductive pathway of AhpE via mycothiol. Free Radic. Biol. Med. 97 (2016) 588-601. [PMID: 27417938]
5. Pedre, B., van Bergen, L.A., Pallo, A., Rosado, L.A., Dufe, V.T., Molle, I.V., Wahni, K., Erdogan, H., Alonso, M., Proft, F.D. and Messens, J. The active site architecture in peroxiredoxins: a case study on Mycobacterium tuberculosis AhpE. Chem. Commun. (Camb.) 52 (2016) 10293-10296. [PMID: 27471753]
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, PDB, 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]
Accepted name: 3-methyl-L-tyrosine peroxygenase
Reaction: 3-methyl-L-tyrosine + H2O2 = 3-hydroxy-5-methyl-L-tyrosine + H2O
For diagram of reaction click here.
Other name(s): SfmD; SacD; 3-methyltyrosine peroxidase; 3-methyl-L-tyrosine peroxidase
Systematic name: 3-methyl-L-tyrosine:hydrogen-peroxide oxidoreductase (3-hydroxy-5-methyl-L-tyrosine-forming)
Comments: The heme-containing peroxygenase from the bacterium Streptomyces lavendulae is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Tang, M.C., Fu, C.Y. and Tang, G.L. Characterization of SfmD as a heme peroxidase that catalyzes the regioselective hydroxylation of 3-methyltyrosine to 3-hydroxy-5-methyltyrosine in saframycin A biosynthesis. J. Biol. Chem. 287 (2012) 5112-5121. [PMID: 22187429]
Accepted name: L-tyrosine peroxygenase
Reaction: L-tyrosine + H2O2 = L-dopa + H2O
Systematic name: L-tyrosine:hydrogen-peroxide oxidoreductase (L-dopa-forming)
Comments: The enzyme from the bacterium Streptomyces lincolnensis participates in the biosynthesis of the antibiotic lincomycin A, while that from Streptomyces refuineus is involved in anthramycin biosynthesis. The enzyme, which contains a heme b cofactor, is rapidly inactivated in the presence of hydrogen peroxide, but the presence of L-tyrosine protects it. cf. EC 1.11.2.5, 3-methyl-L-tyrosine peroxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Neusser, D., Schmidt, H., Spizek, J., Novotna, J., Peschke, U., Kaschabeck, S., Tichy, P. and Piepersberg, W. The genes lmbB1 and lmbB2 of Streptomyces lincolnensis encode enzymes involved in the conversion of L-tyrosine to propylproline during the biosynthesis of the antibiotic lincomycin A. Arch. Microbiol. 169 (1998) 322-332. [PMID: 9531633]
2. Connor, K.L., Colabroy, K.L. and Gerratana, B. A heme peroxidase with a functional role as an L-tyrosine hydroxylase in the biosynthesis of anthramycin. Biochemistry 50 (2011) 8926-8936. [PMID: 21919439]
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, PDB, 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, PDB, 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, PDB, 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, EAWAG-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, PDB, 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, EAWAG-BBD, 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. 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 + oxidized coenzyme F420 = reduced coenzyme F420
For diagram of reaction click here
Glossary: coenzyme F420
Other name(s): 8-hydroxy-5-deazaflavin-reducing hydrogenase; F420-reducing hydrogenase; coenzyme F420-dependent hydrogenase
Systematic name: hydrogen:coenzyme F420 oxidoreductase
Comments: An iron-sulfur flavoprotein (FAD) containing nickel. The enzyme from some sources contains selenocysteine. The enzyme also reduces the riboflavin analogue of F420, flavins and methylviologen, but to a lesser extent. The hydrogen acceptor coenzyme F420 is a deazaflavin derivative.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, 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 + (sulfide)n = hydrogen sulfide + (sulfide)n-1
Other name(s): sulfur reductase
Systematic name: H2:polysulfide oxidoreductase
Comments: An iron-sulfur protein. The enzyme from the hyperthermophilic archaeon Pyrococcus furiosus is part of two heterotetrameric complexes where the β and γ subunits function as sulfur reductase and the α and δ subunits function as hydrogenases (EC 1.12.1.3, hydrogen dehydrogenase [NADP+] and EC 1.12.1.4, hydrogen dehydrogenase [NAD(P)+], respectively). Sulfur can also be used as substrate, but since it is insoluble in aqueous solution and polysulfide is generated abiotically by the reaction of hydrogen sulfide and sulfur, polysulfide is believed to be the true substrate [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 101637-43-8
References:
1. Zöphel, A., Kennedy, M.C., Beinert, H. and Kroneck, P.M.H. Investigations on microbial sulfur respiration. 1. Activation and reduction of elemental sulfur in several strains of Eubacteria. Arch. Microbiol. 150 (1988) 72-77.
2. Ma, K., Schicho, R.N., Kelly, R.M. and Adams, M.W. Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: evidence for a sulfur-reducing hydrogenase ancestor. Proc. Natl. Acad. Sci. USA 90 (1993) 5341-5344. [PMID: 8389482]
3. Ma, K., Zhou, Z.H. and Adams, M.W. Hydrogen production from pyruvate by enzymes purified from the hyperthermophilic archaeon, Pyrococcus furiosus: A key role for NADPH. FEMS Microbiol. Lett. 122 (1994) 245-250.
4. Ma, K., Weiss, R. and Adams, M.W. Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction. J. Bacteriol. 182 (2000) 1864-1871. [PMID: 10714990]
[EC 1.12.99.2 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 + acceptor = reduced acceptor
Other name(s): H2 producing hydrogenase[ambiguous]; hydrogen-lyase[ambiguous]; hydrogenlyase[ambiguous]; uptake hydrogenase[ambiguous]; hydrogen:(acceptor) oxidoreductase
Systematic name: hydrogen:acceptor oxidoreductase
Comments: Uses molecular hydrogen for the reduction of a variety of substances. Contains iron-sulfur clusters. The enzyme from some sources contains nickel.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9027-05-8
References:
1. Shug, A.L., Wilson, P.W., Green, D.E. and Mahler, H.R. The role of molybdenum and flavin in hydrogenase. J. Am. Chem. Soc. 76 (1954) 3355-3356.
2. Adams, M.W.W., Mortenson, L.E. and Chen, J.S. Hydrogenase. Biochim. Biophys. Acta 594 (1981) 105-176.
3. Vignais, P.M., Billoud, B. and Meyer, J. Classification and phylogeny of hydrogenases. FEMS Microbiol. Rev. 25 (2001) 455-501. [PMID: 11524134]