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TitleActive site modifications in pentaerythritol tetranitrate reductase can lead to improved product enantiopurity, decreased by-product formation and altered stereochemical outcome in reactions with a,b-unsaturated nitroolefins
Journal, issue, pagesCatalysis Science and Technology, Year 2011
Publish dateOct 13, 2010 (structure data deposition date)
AuthorsFryszkowska, A. / Toogood, H.S. / Sakuma, M. / Stephens, G.M. / Gardiner, J.M. / Scrutton, N.S.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1 - 1.19 Å
Structure data

PDB-3p84:
Y351A mutant of pentaerythritol tetranitrate reductase containing a bound acetate molecule
Method: X-RAY DIFFRACTION / Resolution: 1.1 Å

PDB-3p8i:
Y351F mutant of pentaerythritol tetranitrate reductase containing a bound acetate molecule
Method: X-RAY DIFFRACTION / Resolution: 1.19 Å

PDB-3p8j:
Y351S mutant of pentaerythritol tetranitrate reductase containing a bound acetate molecule
Method: X-RAY DIFFRACTION / Resolution: 1 Å

Chemicals

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

Source
  • enterobacter cloacae (bacteria)
KeywordsOXIDOREDUCTASE / old yellow enzyme family / alpha / beta barrel

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