Active-site Arg → Lys substitutions alter reaction and substrate specificity of aspartate aminotransferase

Journal of Biological Chemistry

Volumn 272, Issue 35, 1997, Pages 21932-21937

  Vacca, Rosa Anna ^a   Giannattasio, Sergio ^a   Graber, Rachel ^b   Sandmeier, Erika ^b   Marra, Ersilia ^a   Christen, Philipp ^b  

^a CNR   (Italy)

^b UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

AMINOTRANSFERASE; ARGININE; ASPARTATE AMINOTRANSFERASE; LYSINE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; DECARBOXYLATION; ENZYME ACTIVITY; ENZYME BINDING; ENZYME MECHANISM; ENZYME SPECIFICITY; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS;

ARGININE; ASPARTATE AMINOTRANSFERASES; BINDING SITES; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; LYSINE; MODELS, CHEMICAL; MUTAGENESIS, SITE-DIRECTED; SPECTROPHOTOMETRY; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

FELIS CATUS;

EID: 0030822630     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.35.21932     Document Type: Article

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