Making an Oriental equivalent of the yeast cytosolic aldehyde dehydrogenase as well as making one with positive cooperativity in coenzyme binding by mutations of glutamate 492 and arginine 480

Chemico-Biological Interactions

Volumn 130-132, Issue , 2001, Pages 173-179

  Wei, Baoxian ^a   Weiner, Henry ^a  

^a PURDUE UNIVERSITY   (United States)

Author keywords

Aldehyde dehydrogenase; Cooperativity; Oriental variant; Yeast

Indexed keywords

ALDEHYDE DEHYDROGENASE; ARGININE; GLUTAMIC ACID; MITOCHONDRIAL ENZYME;

ALCOHOL METABOLISM; AMINO ACID SUBSTITUTION; COENZYME; CONFERENCE PAPER; ENZYME ANALYSIS; ENZYME BINDING; ENZYME KINETICS; GENE DISRUPTION; GENE MUTATION; MUTAGENESIS; SACCHAROMYCES CEREVISIAE; SEQUENCE ANALYSIS; YEAST;

ALDEHYDE DEHYDROGENASE; AMINO ACID SEQUENCE; ARGININE; BINDING SITES; COENZYMES; CYTOSOL; GLUTAMIC ACID; HUMANS; ISOENZYMES; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NADP; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY, AMINO ACID;

SACCHAROMYCES CEREVISIAE;

EID: 0035969881     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(00)00232-5     Document Type: Conference Paper

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