On https://www.uniprot.org/uniprot/P07524, tyrosinase is shown as a monophenol monooxygenase. However, the UniProt database only shows a metal (copper) binding site, when there is presumed to be an actual active site that performs the reactions, other than the metal binding site. Are there any clues to find the actual reaction active site for a monooxygenase? Please include the sources, if there are.

  • $\begingroup$ Your question is a bit low on information. Is this the exact protein you're working on? The uniprot website states that all the information is inferred from homology, did you check homologous proteins? Did you check if more information is available for closely related proteins? $\endgroup$ – VonBeche Jan 18 '18 at 17:00

Tyrosinase uses two copper ions as cofactors. The copper binding site is the enzyme active site.

The active site of the crystal structure of tyrosinase from Streptomyces sp. (PDB code: 3AWT) is shown below. Note the two copper ions (coordinated by active site histidine amino acid residues) and an oxygen atom (of a water molecule) bound to the copper ions: enter image description here

Matoba et al. (2011) J Biol Chem 34: 30219-30231.

The Cu(II)-soaked crystal structure of tyrosinase ... possesses two copper ions at its catalytic center.


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