Steroid-binding site residues dictate optimal substrate positioning in rat 3α-hydroxysteroid dehydrogenase (3α-HSD or AKR1C9)

Chemico-Biological Interactions

Volumn 143-144, Issue , 2003, Pages 393-400

  Heredia, Vladi V ^a   Kruger, Ryan G ^a   Penning, Trevor M ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

3 Hydroxysteroid dehydrogenase; Alanine scanning mutagenesis; Aldo keto reductase; Substrate recognition

Indexed keywords

20ALPHA HYDROXYSTEROID DEHYDROGENASE; 3ALPHA HYDROXYSTEROID DEHYDROGENASE; ALANINE; CIS ACTING ELEMENT; LIVER ENZYME; OXIDOREDUCTASE; PROGESTERONE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; STEROID HORMONE; TESTOSTERONE; TESTOSTERONE 17BETA DEHYDROGENASE; TRANS ACTING FACTOR; TRYPTOPHAN;

AMINO ACID SUBSTITUTION; CATALYSIS; CATALYST; CONFERENCE PAPER; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ANALYSIS; ENZYME BINDING; ENZYME STRUCTURE; ENZYME SUBSTRATE; FLUORESCENCE; FLUOROMETRY; MOLECULAR BIOLOGY; NONHUMAN; PROTEIN FAMILY; PROTEIN FUNCTION; RAT; SPECTROPHOTOMETRY; STEROID BINDING; TITRIMETRY; WILD TYPE;

ALANINE; ANIMALS; BINDING SITES; HYDROXYSTEROID DEHYDROGENASES; KINETICS; PROGESTERONE; RATS; SUBSTRATE SPECIFICITY; TESTOSTERONE;

RODENTIA;

EID: 0037330959     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(02)00176-X     Document Type: Conference Paper

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