PROSITE documentation PDOC00398

Tyrosinase signatures

Description

Tyrosinase (EC 1.14.18.1) [1] is a copper monooxygenases that catalyzes 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 ion 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:

  • 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.
  • TRP-2 (TYRP2) [6], which is the melanogenic enzyme DOPAchrome tautomerase (EC 5.3.3.12) that catalyzes 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:

  • Plants polyphenol oxidases (PPO) (EC 1.10.3.1) which catalyze the oxidation of mono- and o-diphenols to o-diquinones [8].
  • Caenorhabditis elegans hypothetical protein C02C2.1.

We have derived two signature patterns for tyrosinase and related proteins. The first one contains two of the histidines that bind CuA, and is located in the N-terminal section of tyrosinase. The second pattern contains a histidine that binds CuB, that pattern is located in the central section of the enzyme.

Last update:

April 2006 / Pattern revised.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

TYROSINASE_1, PS00497; Tyrosinase CuA-binding region signature  (PATTERN)
Consensus pattern: H-x(4,5)-F-[LIVMFTP]-x-[FW]-H-R-x(2)-[LVMT]-x(3)-E
The 2 H's are copper ligands
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00497
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00497
• Scan Swiss-Prot/TrEMBL entries against PS00497
• view ligand binding statistics
Matching PDB structures: 1BT1 1BT2 1BT3 1BUG ... [ALL]
TYROSINASE_2, PS00498; Tyrosinase and hemocyanins CuB-binding region signature  (PATTERN)
Consensus pattern: D-P-x-F-[LIVMFYW]-x(2)-H-x(3)-D
H is a copper ligand
Sequences known to belong to this class detected by the pattern: ALL the tyrosinases as well as all the hemocyanins
Other sequence(s) detected in Swiss-Prot: NONE.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00498
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00498
• Scan Swiss-Prot/TrEMBL entries against PS00498
• view ligand binding statistics
Matching PDB structures: 1HC1 1HCY 1JS8 1LL1 ... [ALL]

References

1 Authors Lerch K.
Title Protein and active-site structure of tyrosinase.
Source Prog. Clin. Biol. Res. 256:85-98(1988).
PubMed ID 3130643
2 Authors Jackman M.P., Hajnal A., Lerch K.
Title Albino mutants of Streptomyces glaucescens tyrosinase.
Source Biochem. J. 274:707-713(1991).
PubMed ID 1901488
3 Authors Linzen B.
Title Blue blood: structure and evolution of hemocyanin.
Source Naturwissenschaften 76:206-211(1989).
PubMed ID 2664531
4 Authors Lang W.H., van Holde K.E.
Title Cloning and sequencing of Octopus dofleini hemocyanin cDNA: derived sequences of functional units Ode and Odf.
Source Proc. Natl. Acad. Sci. U.S.A. 88:244-248(1991).
PubMed ID 1898774
5 Authors Kobayashi T., Urabe K., Winder A., Jimenez-Cervantes C., Imokawa G., Brewington T., Solano F., Garcia-Borron J.C., Hearing V.J.
Title Tyrosinase related protein 1 (TRP1) functions as a DHICA oxidase in melanin biosynthesis.
Source EMBO J. 13:5818-5825(1994).
PubMed ID 7813420
6 Authors Jackson I.J., Chambers D.M., Tsukamoto K., Copeland N.G., Gilbert D.J., Jenkins N.A., Hearing V.
Title A second tyrosinase-related protein, TRP-2, maps to and is mutated at the mouse slaty locus.
Source EMBO J. 11:527-535(1992).
PubMed ID 1537334
7 Authors Solano F., Martinez-Liarte J.H., Jimenez-Cervantes C., Garcia-Borron J.C., Lozano J.A.
Title Dopachrome tautomerase is a zinc-containing enzyme.
Source Biochem. Biophys. Res. Commun. 204:1243-1250(1994).
PubMed ID 7980602
8 Authors Cary J.W., Lax A.R., Flurkey W.H.
Title Cloning and characterization of cDNAs coding for Vicia faba polyphenol oxidase.
Source Plant Mol. Biol. 20:245-253(1992).
PubMed ID 1391768

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