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TitleMutation at a strictly conserved, active site tyrosine in the copper amine oxidase leads to uncontrolled oxygenase activity.
Journal, issue, pagesBiochemistry, Vol. 49, Page 7393-7402, Year 2010
Publish dateMay 30, 2010 (structure data deposition date)
AuthorsChen, Z.W. / Datta, S. / Dubois, J.L. / Klinman, J.P. / Mathews, F.S.
External linksBiochemistry / PubMed:20684524
MethodsX-ray diffraction
Resolution1.9 - 2.5 Å
Structure data

PDB-3n9h:
Crystal Structural of mutant Y305A in the copper amine oxidase from hansenula polymorpha
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-3nbb:
Crystal structure of mutant Y305F expressed in E. coli in the copper amine oxidase from hansenula polymorpha
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-3nbj:
Crystal Structure of Y305F mutant of the copper amine oxidase from Hansenula polymorpha expressed in yeast
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-CU:
COPPER (II) ION

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

Source
  • pichia angusta (fungus)
KeywordsOXIDOREDUCTASE / amine oxidase / quinoprotein

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