The reaction catalyzed by Escherichia coli aspartate aminotransferase has multiple partially rate-determining steps, while that catalyzed by the Y225F mutant is dominated by ketimine hydrolysis

Biochemistry

Volumn 35, Issue 16, 1996, Pages 5280-5291

  Goldberg, Jonathan M ^a,b   Kirsch, Jack F ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b STANFORD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINOKETONE; ASPARTATE AMINOTRANSFERASE; ASPARTIC ACID; BACTERIAL ENZYME; DEUTERIUM; HYDROGEN; MUTANT PROTEIN; OXALOACETIC ACID; OXOACID; PHENYLALANINE; TYROSINE;

ARTICLE; ENZYME MECHANISM; ESCHERICHIA COLI; HYDROGEN BOND; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; SITE DIRECTED MUTAGENESIS; TRANSAMINATION;

ASPARTATE AMINOTRANSFERASES; ASPARTIC ACID; CATALYSIS; COMPUTER SIMULATION; DEUTERIUM; DIFFUSION; ESCHERICHIA COLI; EVOLUTION; HYDROLYSIS; IMINES; KINETICS; MODELS, CHEMICAL; MUTATION; OXALOACETATES; OXALOACETIC ACIDS; SOLVENTS; SPECTROPHOTOMETRY; THERMODYNAMICS; TRANSAMINASES; VISCOSITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; FELIS CATUS;

EID: 0029981787     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi952138d     Document Type: Article

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