The crystal structure of the GCY1 protein from S. Cerevisiae suggests a divergent aldo-keto reductase catalytic mechanism

Chemico-Biological Interactions

Volumn 130-132, Issue , 2001, Pages 527-536

  Hur, Eugene ^a   Wilson, David K ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Aldo keto reductase; Crystal structure; Gcy1p

Indexed keywords

ALDEHYDE REDUCTASE; GENE PRODUCT; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

BINDING AFFINITY; CATALYSIS; CONFERENCE PAPER; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME SUBSTRATE; MICHAELIS CONSTANT; NONHUMAN; PROTEIN STRUCTURE; SACCHAROMYCES CEREVISIAE;

ALCOHOL OXIDOREDUCTASES; BASE SEQUENCE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DNA PRIMERS; FUNGAL PROTEINS; MODELS, MOLECULAR; NADP; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE;

SACCHAROMYCES CEREVISIAE;

EID: 0035969879     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(00)00296-9     Document Type: Article

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8. + channel β subunit
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