D
IPR002227

Tyrosinase copper-binding domain

InterPro entry
Short nameTyrosinase_Cu-bd
Overlapping
homologous
superfamilies
 

Description

Tyrosinase (
1.14.18.1
)
[1]
is a copper monooxygenases that catalyses the hydroxylation of monophenols and the oxidation of o-diphenols to o-quinols. This enzyme, found in prokaryotes as well as in eukaryotes, is involved in the formation of pigments such as melanins and other polyphenolic compounds. Tyrosinase binds two copper ions (CuA and CuB). Each of the two copper ions has been shown
[2]
to be bound by three conserved histidines residues. The regions around these copper-binding ligands are well conserved and also shared by some hemocyanins, which are copper-containing oxygen carriers from the hemolymph of many molluscs and arthropods
[3, 4]
. At least two proteins related to tyrosinase are known to exist in mammals, and include TRP-1 (TYRP1)
[5]
, which is responsible for the conversion of 5,6-dihydro-xyindole-2-carboxylic acid (DHICA) to indole-5,6-quinone-2-carboxylic acid; and TRP-2 (TYRP2)
[6]
, which is the melanogenic enzyme DOPAchrome tautomerase (
5.3.3.12
) that catalyses the conversion of DOPAchrome to DHICA. TRP-2 differs from tyrosinases and TRP-1 in that it binds two zinc ions instead of copper
[7]
. Other proteins that belong to this family are plant polyphenol oxidases (PPO) (
1.10.3.1
), which catalyze the oxidation of mono- and o-diphenols to o-diquinones
[8]
; and Caenorhabditis elegans hypothetical protein C02C2.1.

References

1.Protein and active-site structure of tyrosinase. Lerch K. Prog. Clin. Biol. Res. 256, 85-98, (1988). PMID: 3130643

2.Albino mutants of Streptomyces glaucescens tyrosinase. Jackman MP, Hajnal A, Lerch K. Biochem. J. 274 ( Pt 3), 707-13, (1991). View articlePMID: 1901488

3.[Blue blood: structure and evolution of hemocyanin] Linzen B. Naturwissenschaften 76, 206-11, (1989). View articlePMID: 2664531

4.Cloning and sequencing of Octopus dofleini hemocyanin cDNA: derived sequences of functional units Ode and Odf. Lang WH, van Holde KE. Proc. Natl. Acad. Sci. U.S.A. 88, 244-8, (1991). View articlePMID: 1898774

5.Tyrosinase related protein 1 (TRP1) functions as a DHICA oxidase in melanin biosynthesis. Kobayashi T, Urabe K, Winder A, Jimenez-Cervantes C, Imokawa G, Brewington T, Solano F, Garcia-Borron JC, Hearing VJ. EMBO J. 13, 5818-25, (1994). View articlePMID: 7813420

6.A second tyrosinase-related protein, TRP-2, maps to and is mutated at the mouse slaty locus. Jackson IJ, Chambers DM, Tsukamoto K, Copeland NG, Gilbert DJ, Jenkins NA, Hearing V. EMBO J. 11, 527-35, (1992). View articlePMID: 1537334

7.Dopachrome tautomerase is a zinc-containing enzyme. Solano F, Martinez-Liarte JH, Jimenez-Cervantes C, Garcia-Borron JC, Lozano JA. Biochem. Biophys. Res. Commun. 204, 1243-50, (1994). View articlePMID: 7980602

8.Cloning and characterization of cDNAs coding for Vicia faba polyphenol oxidase. Cary JW, Lax AR, Flurkey WH. Plant Mol. Biol. 20, 245-53, (1992). View articlePMID: 1391768

GO terms

biological process

  • None

cellular component

  • None

Cross References

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