Increasing the reaction rate of hydroxynitrile lyase from hevea brasiliensis toward mandelonitrile by copying active site residues from an esterase that accepts aromatic esters

ChemBioChem

Volumn 15, Issue 13, 2014, Pages 1931-1938

  Von Langermann, Jan ^a,b   Nedrud, David M ^a   Kazlauskas, Romas J ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

^b UNIVERSITY OF ROSTOCK   (Germany)

Author keywords

enzyme catalysis; esterases; hydroxynitrile lyase; promiscuous activity; protein engineering

Indexed keywords

ALANINE; AROMATIC ESTER; BENZALDEHYDE; BINDING PROTEIN; CITRIC ACID; CYANOHYDRIN; CYSTEINE; ESTER DERIVATIVE; ESTERASE; GLYCINE; HYDROGEN CYANIDE; HYDROXYNITRILE LYASE; MANDELONITRILE; NITRILE; PROLINE; SALICYLIC ACID BINDING PROTEIN 2; TERT BUTYL METHYL ETHER; UNCLASSIFIED DRUG; VALINE; ACETONITRILE DERIVATIVE; AROMATIC HYDROCARBON; ESTER; LYASE; MANDELONITRILE LYASE; SABP2 PROTEIN, NICOTIANA TABACUM; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; BIOCATALYSIS; ENANTIOMER; ENANTIOSELECTIVITY; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME SPECIFICITY; HEVEA BRASILIENSIS; HYDROGEN BOND; HYDROLYSIS; MOLECULAR MODEL; NICOTIANA BENTHAMIANA; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN UNFOLDING; SITE DIRECTED MUTAGENESIS; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GENETICS; HEVEA; STEREOISOMERISM;

HEVEA BRASILIENSIS;

ACETONITRILES; ALDEHYDE-LYASES; CATALYSIS; CATALYTIC DOMAIN; ESTERASES; ESTERS; HEVEA; HYDROCARBONS, AROMATIC; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PLANT PROTEINS; PROTEIN UNFOLDING; STEREOISOMERISM; SUBSTRATE SPECIFICITY;

EID: 84907668884     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.201402081     Document Type: Article

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