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TitleSubstrate binding in the FAD-dependent hydroxynitrile lyase from almond provides insight into the mechanism of cyanohydrin formation and explains the absence of dehydrogenation activity.
Journal, issue, pagesBiochemistry, Vol. 48, Page 3370-3377, Year 2009
Publish dateFeb 24, 2009 (structure data deposition date)
AuthorsDreveny, I. / Andryushkova, A.S. / Glieder, A. / Gruber, K. / Kratky, C.
External linksBiochemistry / PubMed:19256550
MethodsX-ray diffraction
Resolution1.57 - 1.67 Å
Structure data

PDB-3gdn:
Almond hydroxynitrile lyase in complex with benzaldehyde
Method: X-RAY DIFFRACTION / Resolution: 1.67 Å

PDB-3gdp:
Hydroxynitrile lyase from almond, monoclinic crystal form
Method: X-RAY DIFFRACTION / Resolution: 1.57 Å

Chemicals

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

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-HBX:
benzaldehyde

ChemComp-MXN:
(2R)-hydroxy(phenyl)ethanenitrile

ChemComp-HOH:
WATER

ChemComp-IPA:
ISOPROPYL ALCOHOL / alkaloid*YM

ChemComp-NDG:
2-acetamido-2-deoxy-alpha-D-glucopyranose

Source
  • prunus dulcis (almond)
KeywordsLYASE / HYDROXYNITRILE LYASE / FLAVIN / GMC OXIDOREDUCTASE / ALMOND / CYANOGENESIS / Flavoprotein

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