IUBMB Enzyme Nomenclature


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 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


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]

[EC created 1961, deleted 1972, reinstated 1978]

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