EC 1.10.3.2 - Laccase

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IntEnz Enzyme Nomenclature
EC 1.10.3.2

Names

Accepted name:
laccase
Other names:
p-diphenol oxidase
urishiol oxidase
urushiol oxidase
Systematic name:
benzenediol:oxygen oxidoreductase

Reaction

Cofactor

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UM-BBD , UniPathway
Protein domains and families: PROSITE:PDOC00076
Structural data: CSA , EC2PDB
Gene Ontology: GO:0052716
CAS Registry Number: 80498-15-3
UniProtKB/Swiss-Prot: (88) [show] [UniProt]

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, 454-498
  2. Keilin, D. and Mann, T.
    Laccase, a blue copper-protein oxidase from the latex of Rhus succedanea.
    Nature (Lond.) 143: 23-24 (1939).
  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, 507-579
  4. Mayer, A.M. and Harel, E.
    Polyphenol oxidases in plants.
    Phytochemistry 18: 193-215 (1979).
  5. Nakamura, T.
    Purification and physico-chemical properties of laccase.
    Biochim. Biophys. Acta 30: 44-52 (1958).
  6. Nakamura, T.
    Stoichiometric studies on the action of laccase.
    Biochim. Biophys. Acta 30: 538-542 (1958).
  7. Peisach, J. and Levine, W.G.
    A comparison of the enzymic activities of pig ceruloplasmin and Rhus vernicifera laccase.
    J. Biol. Chem. 240: 2284-2289 (1965).
  8. Reinhammar, B. and Malmström, B.G.
    "Blue" copper-containing oxidases.
    In: Spiro, T.G. (Ed.) Copper Proteins, Wiley, New York, 1981, 109-149

[EC 1.10.3.2 created 1961, deleted 1972, reinstated 1978]