EC - Catechol oxidase

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IntEnz Enzyme Nomenclature


Accepted name:
catechol oxidase
Other names:
o-diphenol oxidoreductase
o-diphenol:oxygen oxidoreductase
Dopa oxidase
diphenol oxidase
polyphenol oxidase
pyrocatechol oxidase
Systematic name:
1,2-benzenediol:oxygen oxidoreductase




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, which can catalyse both the monooxygenation of monophenols and the oxidation of catechols.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00398
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004097
CAS Registry Number: 9002-10-2
UniProtKB/Swiss-Prot: (15) [show] [UniProt]


  1. Brown, F.C. and Ward, D.N.
    Preparation of a soluble mammalian tyrosinase.
    J. Am. Chem. Soc. 79 : 2647-2648 (1957).
  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 , 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 : 569-581 (1966).
  4. Mason, H.S.
    Structures and functions of the phenolase complex.
    Nature 177 : 79-81 (1956).
  5. Mayer, A.M. and Harel, E.
    Polyphenol oxidases in plants.
    Phytochemistry 18 : 193-215 (1979).
  6. Patil, S.S. and Zucker, M.
    Potato phenolases. Purification and properties.
    J. Biol. Chem. 240 : 3938-3943 (1965). [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 : 5308-5314 (1967). [PMID: 4965136]
  8. Robb, D.A.
    In: Lontie, R. (Ed.) Copper Proteins and Copper Enzymes vol. 2 , CRC Press , Boca Raton, FL , 1984 , 207-240

[EC created 1961, deleted 1972, reinstated 1978]