Mutation of arginine 98, which serves as a substrate-recognition site of D-amino acid aminotransferase, can be partly compensated for by mutation of tyrosine 88 to an arginyl residue

Journal of Biochemistry

Volumn 122, Issue 6, 1997, Pages 1182-1189

  Kishimoto, Kazuhisa ^a   Yoshimura, Tohru ^a   Soda, Kenji ^b   Esaki, Nobuyoshi ^a  

^a KYOTO UNIVERSITY   (Japan)

^b KANSAI UNIVERSITY   (Japan)

Author keywords

Carboxyl binding site for substrates; D amino acid aminotransferase; Inhibition by ketoglutarate; Site directed mutagenesis

Indexed keywords

2 OXOGLUTARIC ACID; AMINOTRANSFERASE; ARGININE; DEXTRO AMINO ACID AMINOTRANSFERASE; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CONTROLLED STUDY; ENZYME BINDING; ENZYME INHIBITION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; GENE MUTATION; PH; SITE DIRECTED MUTAGENESIS; STEREOSPECIFICITY; STRUCTURE ACTIVITY RELATION; TRANSAMINATION; X RAY CRYSTALLOGRAPHY;

EID: 0031474880     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021879     Document Type: Article

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