Substrate binding in the FAD-dependent hydroxynitrile lyase from almond provides insight into the mechanism of cyanohydrin formation and explains the absence of dehydrogenation activity

Biochemistry

Volumn 48, Issue 15, 2009, Pages 3370-3377

  Dreveny, Ingrid ^a,c   Andryushkova, Aleksandra S ^b   Glieder, Anton ^b   Gruber, Karl ^a   Kratky, Christoph ^a  

^a UNIVERSITY OF GRAZ   (Austria)

^b GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

^c UNIVERSITY OF NOTTINGHAM   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE ARCHITECTURES; ACTIVE SITES; BINDING GEOMETRIES; COMMON FEATURES; ELECTROSTATIC POTENTIALS; FLAVIN COFACTOR; GENERAL BASE; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE; HISTIDINE RESIDUES; HYDROGEN CYANIDES; HYDROXYL GROUPS; HYDROXYNITRILE LYASE; HYDROXYNITRILE LYASES; IN-VITRO; PLANT SPECIES; REACTION MECHANISMS; REACTION PRODUCTS; SITE-DIRECTED MUTAGENESIS; STEREOSPECIFIC SYNTHESIS; STRUCTURAL DATUM; SUBSTRATE BINDINGS; SUBSTRATE SPECIFICITIES; TISSUE DAMAGES;

ALDEHYDES; CYANIDES; DEHYDROGENATION; ENZYMES; GLUCOSE; HYDROGEN; METHANOL; SUBSTRATES;

BINDING SITES;

BENZALDEHYDE; CYANOHYDRIN; FLAVINE ADENINE NUCLEOTIDE; HISTIDINE; HYDROXYL GROUP; HYDROXYNITRILE LYASE; PROTON; QUERCETIN;

ALMOND; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DEHYDROGENATION; ELECTRIC CAPACITANCE; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

ACETONITRILES; ALDEHYDE-LYASES; BINDING SITES; CATALYSIS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; FLAVIN-ADENINE DINUCLEOTIDE; HYDROGENATION; LIGANDS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NITRILES; PRUNUS; SUBSTRATE SPECIFICITY;

FUNGI; PRUNUS DULCIS;

EID: 65249128570     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802162s     Document Type: Article

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