Analysis of the substrate-recognition mode of aromatic amino acid aminotransferase by combined use of quasisubstrates and site-directed mutagenesis: Systematic hydroxy-group addition/deletion studies to probe the enzyme - Substrate interactions

Biochemistry

Volumn 35, Issue 21, 1996, Pages 6754-6761

  Hayashi, Hideyuki ^a   Inoue, Katsura ^a   Mizuguchi, Hiroyuki ^a   Kagamiyama, Hiroyuki ^a  

^a OSAKA MEDICAL COLLEGE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; FELIS CATUS;

AMINOTRANSFERASE; AROMATIC AMINO ACID;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; ENZYME ANALYSIS; ENZYME BINDING; ENZYME CONFORMATION; ENZYME SUBSTRATE; ESCHERICHIA COLI; HYDROXYLATION; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; REACTION ANALYSIS; SITE DIRECTED MUTAGENESIS; TRANSAMINATION;

AMINO ACID SEQUENCE; BASE SEQUENCE; BINDING SITES; KINETICS; LIGANDS; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OLIGODEOXYRIBONUCLEOTIDES; POINT MUTATION; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE DELETION; TRANSAMINASES;

EID: 0030008569     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi960390v     Document Type: Article

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