Dissection of the physiological interconversion of 5α-DHT and 3α-diol by rat 3α-HSD via transient kinetics shows that the chemical step is rate-determining: Effect of mutating cofactor and substrate-binding pocket residues on catalysis

Biochemistry

Volumn 43, Issue 38, 2004, Pages 12028-12037

  Heredia, Vladi V ^a   Penning, Trevor M ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CHEMICAL BONDS; DATA REDUCTION; FLUORESCENCE; ISOTOPES; METABOLITES; OXIDATION; PROTEINS; REACTION KINETICS;

ANDROGEN METABOLITE; CHEMICAL TRANSFORMATIONS; KINETIC ISOTOPES; PHASE KINETICS;

BIOLOGICAL ORGANS;

3ALPHA HYDROXYSTEROID DEHYDROGENASE; ADENOSINE 2' PHOSPHATE; ALANINE; ANDROSTANEDIOL; ANDROSTANOLONE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING SITE; CATALYSIS; CHEMICAL REACTION KINETICS; ENZYME SUBSTRATE COMPLEX; FLUORESCENCE; HYDROPHOBICITY; MUTATION; NONHUMAN; OXIDATION; PRIORITY JOURNAL; RAT; STEROID BINDING;

3-ALPHA-HYDROXYSTEROID DEHYDROGENASE (B-SPECIFIC); ANDROSTANE-3,17-DIOL; ANIMALS; BINDING SITES; CATALYSIS; DIHYDROTESTOSTERONE; ISOTOPES; KINETICS; MOLECULAR STRUCTURE; MUTATION; NADP; OXIDATION-REDUCTION; RATS; SOLVENTS;

FELIS CATUS;

EID: 4644346337     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0489762     Document Type: Article

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