Narrowing substrate specificity in a directly evolved enzyme: The A293D mutant of aspartate aminotransferase

Biochemistry

Volumn 43, Issue 40, 2004, Pages 12780-12787

  Chow, Margaret A ^a   McElroy, Kathryn E ^a   Corbett, Kevin D ^a   Berger, James M ^a   Kirsch, Jack F ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; ENZYME INHIBITION; ESCHERICHIA COLI; MUTAGENESIS; PROTEINS; SUBSTRATES;

DICARBOXYLIC SUBSTRATES; LIGAND COMPLEXES; MUTATION;

ENZYMES;

ASPARTATE AMINOTRANSFERASE; ASPARTIC ACID; DICARBOXYLIC ACID; LIGAND; MUTANT PROTEIN; PHENYLALANINE; PROTEIN SRHEPT; TYROSINE AMINOTRANSFERASE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; LIGAND BINDING; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; QUANTITATIVE ANALYSIS; SITE DIRECTED MUTAGENESIS; WILD TYPE;

ALANINE; ASPARTATE AMINOTRANSFERASES; CRYSTALLOGRAPHY, X-RAY; DIRECTED MOLECULAR EVOLUTION; ESCHERICHIA COLI; KINETICS; MODELS, MOLECULAR; MUTATION; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY; TYROSINE TRANSAMINASE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 4944240750     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0487544     Document Type: Article

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