Site-directed mutagenesis, kinetic and inhibition studies of aspartate ammonia lyase from Bacillus sp. YM55-1

FEBS Journal

Volumn 276, Issue 11, 2009, Pages 2994-3007

  Puthan Veetil, Vinod ^a   Raj, Hans ^a   Quax, Wim J ^a   Janssen, Dick B ^b   Poelarends, Gerrit J ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

^b UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

Aspartase; Aspartate ammonia lyase; Bacillus; Deamination; Enzyme mechanism

Indexed keywords

ASPARAGINE; ASPARTATE AMMONIA LYASE; FUMARIC ACID; HISTONE; LYSINE; SERINE; THREONINE;

ARTICLE; BACILLUS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME INHIBITION; GENE MUTATION; KINETICS; NONHUMAN; PH MEASUREMENT; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; WILD TYPE;

AMINO ACID SUBSTITUTION; ASPARAGINE; ASPARTATE AMMONIA-LYASE; ASPARTIC ACID; BACILLUS; BACTERIAL PROTEINS; BINDING SITES; CATALYSIS; CATALYTIC DOMAIN; CIRCULAR DICHROISM; HISTIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; LYSINE; MALATES; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; NITRO COMPOUNDS; PROPIONIC ACIDS; PROTEIN STRUCTURE, TERTIARY; SERINE; SUBSTRATE SPECIFICITY; THREONINE;

BACILLUS SP.;

EID: 65549156987     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2009.07015.x     Document Type: Article

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