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TitleThe basicity of an active-site water molecule discriminates between tyrosinase and catechol oxidase activity.
Journal, issue, pagesInt. J. Biol. Macromol., Vol. 183, Page 1861-1870, Year 2021
Publish dateJul 8, 2020 (structure data deposition date)
AuthorsMatoba, Y. / Oda, K. / Muraki, Y. / Masuda, T.
External linksInt. J. Biol. Macromol. / PubMed:34089758
MethodsX-ray diffraction
Resolution1.47 - 1.5 Å
Structure data

PDB-7cit:
Crystal structure of tyrosinase from Streptomyces castaneoglobisporus in complex with the caddie protein obtained by soaking in the solution containing Cu(II) and hydroxylamine for 24 h
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-7ciy:
Crystal structure of N191G-mutated tyrosinase from Streptomyces castaneoglobisporus in complex with the caddie protein obtained by soaking in the solution containing Cu(II) and hydroxylamine for 24 h
Method: X-RAY DIFFRACTION / Resolution: 1.47 Å

Chemicals

ChemComp-PEO:
HYDROGEN PEROXIDE

ChemComp-CU:
COPPER (II) ION

ChemComp-NO3:
NITRATE ION

ChemComp-HOH:
WATER

Source
  • streptomyces castaneoglobisporus (bacteria)
KeywordsMETAL BINDING PROTEIN / tyrosinase / catalytic mechanism

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