Mutation of nicotinamide pocket residues in rat liver 3α-hydroxysteroid dehydrogenase reveals different modes of cofactor binding

Biochemistry

Volumn 39, Issue 1, 2000, Pages 102-109

  Ma, Haiching ^a   Ratnam, Kapila ^a,b   Penning, Trevor M ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b GLAXOSMITHKLINE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

3ALPHA HYDROXYSTEROID DEHYDROGENASE; ANDROSTANOLONE; ASPARAGINE; GLUTAMINE; LIVER ENZYME; MUTANT PROTEIN; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SERINE; TYROSINE;

ARTICLE; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; MUTATION; NONHUMAN; PRIORITY JOURNAL; RAT; SITE DIRECTED MUTAGENESIS; STEREOSPECIFICITY;

3-ALPHA-HYDROXYSTEROID DEHYDROGENASE (B-SPECIFIC); 3-HYDROXYSTEROID DEHYDROGENASES; ANIMALS; BINDING SITES; KINETICS; LIVER; MUTAGENESIS, SITE-DIRECTED; NADP; NIACINAMIDE; PROTONS; RATS; RECOMBINANT PROTEINS; STEREOISOMERISM;

EID: 0034635134     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi991659o     Document Type: Article

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