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TitleTwo tyrosine residues, Tyr-108 and Tyr-503, are responsible for the deprotonation of phenolic substrates in vanillyl-alcohol oxidase.
Journal, issue, pagesJ. Biol. Chem., Vol. 292, Page 14668-14679, Year 2017
Publish dateJan 23, 2017 (structure data deposition date)
AuthorsEwing, T.A. / Nguyen, Q.T. / Allan, R.C. / Gygli, G. / Romero, E. / Binda, C. / Fraaije, M.W. / Mattevi, A. / van Berkel, W.J.H.
External linksJ. Biol. Chem. / PubMed:28717004
MethodsX-ray diffraction
Resolution2.8 Å
Structure data

PDB-5mxj:
Structure of the Y108F mutant of vanillyl alcohol oxidase
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-5mxu:
Structure of the Y503F mutant of vanillyl alcohol oxidase
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • penicillium simplicissimum (fungus)
KeywordsOXIDOREDUCTASE / vanillyl alcohol oxidase / Y108F mutant / Y503F mutant

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