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, 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 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.
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. [PMID: 11900522]
[EC 1.10.3.1 created 1961, deleted 1972, reinstated 1978]
 
 


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