The Enzyme Database

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EC 1.10.3.1     
Accepted name: catechol oxidase
Reaction: 2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O
Glossary: catechol = 1,2-benzenediol
Other name(s): diphenol oxidase; o-diphenolase; polyphenol oxidase; 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 catechol (i.e., o-diphenol) to the corresponding o-quinone. The enzyme also acts on a variety of substituted catechols. It is different from tyrosinase, EC 1.14.18.1, which can catalyse both the monooxygenation of monophenols and the oxidation of catechols.
Links to other databases: BRENDA, EXPASY, Gene, 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. (Ed.), The Enzymes, 1st edn, vol. 2, Academic Press, New York, 1951, pp. 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. [PMID: 16742427]
4.  Mason, H.S. Structures and functions of the phenolase complex. Nature (Lond.) 177 (1956) 79–81. [PMID: 13288597]
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, pp. 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. [DOI] [PMID: 11900522]
[EC 1.10.3.1 created 1961, deleted 1972, reinstated 1978]
 
 
EC 1.10.3.2     
Accepted name: laccase
Reaction: 4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O
Other name(s): urishiol oxidase; urushiol oxidase; p-diphenol oxidase
Systematic name: benzenediol:oxygen oxidoreductase
Comments: A group of multi-copper proteins of low specificity acting on both o- and p-quinols, and often acting also on aminophenols and phenylenediamine. The semiquinone may react further either enzymically or non-enzymically.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, Gene, 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. (Ed.), The Enzymes, 1st edn, vol. 2, Academic Press, New York, 1951, pp. 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 edn, vol. 12, Academic Press, New York, 1975, pp. 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. [DOI] [PMID: 13584395]
6.  Nakamura, T. Stoichiometric studies on the action of laccase. Biochim. Biophys. Acta 30 (1958) 538–542. [DOI] [PMID: 13618260]
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. [PMID: 14304827]
8.  Reinhammar, B. and Malmström, B.G. "Blue" copper-containing oxidases. In: Spiro, T.G. (Ed.), Copper Proteins, Copper Proteins, New York, 1981, pp. 109–149.
[EC 1.10.3.2 created 1961, deleted 1972, reinstated 1978]
 
 
EC 1.10.3.3     
Accepted name: L-ascorbate oxidase
Reaction: 4 L-ascorbate + O2 = 4 monodehydroascorbate + 2 H2O
Other name(s): ascorbase; ascorbic acid oxidase; ascorbate oxidase; ascorbic oxidase; ascorbate dehydrogenase; L-ascorbic acid oxidase; AAO; L-ascorbate:O2 oxidoreductase; AA oxidase
Systematic name: L-ascorbate:oxygen oxidoreductase
Comments: A multicopper protein.
Links to other databases: BRENDA, EXPASY, Gene, 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. [DOI] [PMID: 13787201]
2.  Stark, G.R. and Dawson, C.R. Ascorbic acid oxidase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), 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. [DOI] [PMID: 1548698]
[EC 1.10.3.3 created 1961, modified 2011]
 
 
EC 1.10.3.4     
Accepted name: o-aminophenol oxidase
Reaction: 4 2-aminophenol + 3 O2 = 2 2-aminophenoxazin-3-one + 6 H2O
For diagram of reaction, 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, Gene, 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. [PMID: 14170322]
2.  Nair, P.M. and Vining, L.C. Isophenoxazine synthase apoenzyme from Pycnoporus coccineus. Biochim. Biophys. Acta 96 (1965) 318–327. [DOI] [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. [DOI] [PMID: 4166439]
4.  Barry, C.E., 3rd, Nayar, P.G. and Begley, T.P. Phenoxazinone synthase: mechanism for the formation of the phenoxazinone chromophore of actinomycin. Biochemistry 28 (1989) 6323–6333. [PMID: 2477054]
[EC 1.10.3.4 created 1972, modified 2006]
 
 
EC 1.10.3.5     
Accepted name: 3-hydroxyanthranilate oxidase
Reaction: 3-hydroxyanthranilate + O2 = 6-imino-5-oxocyclohexa-1,3-dienecarboxylate + H2O2
Other name(s): 3-hydroxyanthranilic acid oxidase
Systematic name: 3-hydroxyanthranilate:oxygen oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-53-4
References:
1.  Morgan, L.R., Jr., Weimorts, D.M. and Aubert, C.C. Oxidation of 3-hydroxyanthranilic acid by a soluble liver fraction from poikilothermic vertebrates. Biochim. Biophys. Acta 100 (1965) 393–402. [DOI] [PMID: 14347936]
[EC 1.10.3.5 created 1972]
 
 
EC 1.10.3.6     
Accepted name: rifamycin-B oxidase
Reaction: rifamycin B + O2 = rifamycin O + H2O2
Other name(s): rifamycin B oxidase
Systematic name: rifamycin-B:oxygen oxidoreductase
Comments: Acts also on benzene-1,4-diol and, more slowly, on some other p-quinols. Not identical with EC 1.10.3.1 (catechol oxidase), EC 1.10.3.2 (laccase), EC 1.10.3.4 (o-aminophenol oxidase) or EC 1.10.3.5 (3-hydroxyanthranilate oxidase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 84932-52-5
References:
1.  Han, M.H., Seong, B.-L., Son, H.-J. and Mheen, T.-I. Rifamycin B oxidase from Monocillium spp., a new type of diphenol oxidase. FEBS Lett. 151 (1983) 36–40. [DOI] [PMID: 6825839]
[EC 1.10.3.6 created 1986]
 
 
EC 1.10.3.7      
Transferred entry: sulochrin oxidase [(+)-bisdechlorogeodin-forming]. 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: sulochrin oxidase [(+)-bisdechlorogeodin-forming]. Now EC 1.21.3.5, sulochrin oxidase [(-)-bisdechlorogeodin-forming]
[EC 1.10.3.8 created 1986, deleted 2002]
 
 
EC 1.10.3.9     
Accepted name: photosystem II
Reaction: 2 H2O + 2 plastoquinone + 4 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, Gene, KEGG, MetaCyc, PDB
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. [DOI] [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. [DOI] [PMID: 19219048]
[EC 1.10.3.9 created 2011]
 
 
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]
 
 
EC 1.10.3.11     
Accepted name: ubiquinol oxidase (non-electrogenic)
Reaction: 2 ubiquinol + O2 = 2 ubiquinone + 2 H2O
Other name(s): plant alternative oxidase; cyanide-insensitive oxidase; AOX (gene name); ubiquinol oxidase; ubiquinol:O2 oxidoreductase (non-electrogenic)
Systematic name: ubiquinol:oxygen oxidoreductase (non-electrogenic)
Comments: The enzyme, described from the mitochondria of plants and some fungi and protists, is an alternative terminal oxidase that is not sensitive to cyanide inhibition and does not generate a proton motive force. Unlike the electrogenic terminal oxidases that contain hemes (cf. EC 1.10.3.10 and EC 1.10.3.14), this enzyme contains a dinuclear non-heme iron complex. The function of this oxidase is believed to be dissipating excess reducing power, minimizing oxidative stress, and optimizing photosynthesis in response to changing conditions.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc
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. [DOI] [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. [DOI] [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:e1000761 (2010). [DOI] [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. [DOI] [PMID: 22848123]
[EC 1.10.3.11 created 2011, modified 2014]
 
 
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]
 
 
EC 1.10.3.15     
Accepted name: grixazone synthase
Reaction: 2 3-amino-4-hydroxybenzoate + N-acetyl-L-cysteine + 2 O2 = grixazone B + 4 H2O + CO2
For diagram of grixazone biosynthesis, 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, Gene, KEGG, MetaCyc
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. [DOI] [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. [DOI] [PMID: 19268377]
[EC 1.10.3.15 created 2014]
 
 
EC 1.10.3.16     
Accepted name: dihydrophenazinedicarboxylate synthase
Reaction: (1) (1R,6R)-1,4,5,5a,6,9-hexahydrophenazine-1,6-dicarboxylate + O2 = (1R,10aS)-1,4,10,10a-tetrahydrophenazine-1,6-dicarboxylate + H2O2
(2) (1R,10aS)-1,4,10,10a-tetrahydrophenazine-1,6-dicarboxylate + O2 = (5aS)-5,5a-dihydrophenazine-1,6-dicarboxylate + H2O2
(3) (1R,10aS)-1,4,10,10a-tetrahydrophenazine-1-carboxylate + O2 = (10aS)-10,10a-dihydrophenazine-1-carboxylate + H2O2
(4) (1R)-1,4,5,10-tetrahydrophenazine-1-carboxylate + O2 = (10aS)-5,10-dihydrophenazine-1-carboxylate + H2O2
For diagram of enediyne antitumour antibiotic biosynthesis and pyocyanin biosynthesis, 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, Gene, KEGG, MetaCyc, PDB
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. [DOI] [PMID: 23897464]
[EC 1.10.3.16 created 2016]
 
 
EC 1.10.3.17     
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, Gene, KEGG, MetaCyc
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]
[EC 1.10.3.17 created 2019]
 
 


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