Biochemical and structural characterization of a novel bacterial manganese-dependent hydroxynitrile lyase

FEBS Journal

Volumn 280, Issue 22, 2013, Pages 5815-5828

  Hajnal, Ivan ^a,b   Łyskowski, Andrzej ^a   Hanefeld, Ulf ^b   Gruber, Karl ^a,c   Schwab, Helmut ^a,d   Steiner, Kerstin ^a  

^a AUSTRIAN CENTRE OF INDUSTRIAL BIOTECHNOLOGY   (Austria)

^b DELFT UNIVERSITY OF TECHNOLOGY   (Netherlands)

^c UNIVERSITY OF GRAZ   (Austria)

^d GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

Author keywords

bacterial hydroxynitrile lyase; cupin structure; enzyme catalysis; metalloenzyme; site directed mutagenesis

Indexed keywords

BENZALDEHYDE; HYDROXYNITRILE LYASE; MANDELONITRILE; MANGANESE; NITRILE; TERT BUTYL METHYL ETHER; UNCLASSIFIED DRUG;

ACIDOBACTERIUM; AMINO ACID SEQUENCE; ARTICLE; BACTERIAL METABOLISM; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENANTIOMER; ENANTIOSELECTIVITY; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SYNTHESIS; ESCHERICHIA COLI; GENETIC CONSERVATION; GRANULICELLA TUNDRICOLA; HETEROLOGOUS EXPRESSION; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN MOTIF; SEQUENCE HOMOLOGY;

BACTERIAL HYDROXYNITRILE LYASE; CUPIN STRUCTURE; ENZYME CATALYSIS; METALLOENZYME; SITE-DIRECTED MUTAGENESIS;

ACETONITRILES; ACIDOBACTERIA; ALDEHYDE-LYASES; AMINO ACID MOTIFS; BACTERIAL PROTEINS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; HYDROGEN-ION CONCENTRATION; KINETICS; MANGANESE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; STEREOISOMERISM;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 84886592636     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12501     Document Type: Article

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