Loop relaxation, A mechanism that explains the reduced specificity of rabbit 20α-hydroxysteroid dehydrogenase, A member of the aldo-keto reductase superfamily

Journal of Molecular Biology

Volumn 339, Issue 1, 2004, Pages 89-102

  Couture, Jean François ^a   Legrand, Pierre ^a   Cantin, Line ^a   Labrie, Fernand ^a   Luu The, Van ^a   Breton, Rock ^a  

^a LAVAL UNIVERSITY   (Canada)

Author keywords

aldo keto reductase enzymes superfamily; binary and ternary complex structures; HSD, hydroxysteroid dehydrogenase; NADP(H); NADPH, reduced form of nicotinamide adenine dinucleotide phosphate; rabbit 20 hydroxysteroid dehydrogenase; testosterone

Indexed keywords

20ALPHA HYDROXYSTEROID DEHYDROGENASE; ALDEHYDE REDUCTASE; AMINO ACID; ANDROGEN; BENZENE DERIVATIVE; GESTAGEN; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; PHENOL DERIVATIVE; PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; STEROID; TESTOSTERONE;

AMINO ACID SEQUENCE; ARTICLE; BINDING KINETICS; CARBOXY TERMINAL SEQUENCE; CHEMICAL COMPOSITION; CHEMICAL STRUCTURE; FLUORESCENCE; KINETICS; MOLECULAR BIOLOGY; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

ORYCTOLAGUS CUNICULUS;

EID: 2342481140     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.03.035     Document Type: Article

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