Hydroxynitrile Lyases with α/β-Hydrolase Fold: Two Enzymes with Almost Identical 3D Structures but Opposite Enantioselectivities and Different Reaction Mechanisms

ChemBioChem

Volumn 13, Issue 13, 2012, Pages 1932-1939

  Andexer, Jennifer N ^a   Staunig, Nicole ^b   Eggert, Thorsten ^c   Kratky, Christoph ^b   Pohl, Martina ^d   Gruber, Karl ^b  

^a UNIVERSITY OF FREIBURG   (Germany)

^b UNIVERSITY OF GRAZ   (Austria)

^c Evocatal GmbH   (Germany)

^d FORSCHUNGSZENTRUM JÜLICH   (Germany)

Author keywords

Biocatalysis; C C lyase; Enzyme mechanisms; Molecular modeling; X ray crystallography

Indexed keywords

ASPARAGINE; HISTIDINE; HYDROLASE; HYDROXYNITRILE LYASE; SERINE;

ARABIDOPSIS; ARTICLE; CONTROLLED STUDY; ENANTIOSELECTIVITY; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HEVEA BRASILIENSIS; MOLECULAR DOCKING; NONHUMAN; PRIORITY JOURNAL; SIMULATION; X RAY CRYSTALLOGRAPHY;

ALDEHYDE-LYASES; ARABIDOPSIS; CRYSTALLOGRAPHY, X-RAY; HEVEA; MODELS, MOLECULAR; POINT MUTATION; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; STEREOISOMERISM; SUBSTRATE SPECIFICITY;

ARABIDOPSIS THALIANA; HEVEA BRASILIENSIS;

EID: 84865568695     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.201200239     Document Type: Article

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