Structure/function of human type 1 3β-hydroxysteroid dehydrogenase: An intrasubunit disulfide bond in the Rossmann-fold domain and a Cys residue in the active site are critical for substrate and coenzyme utilization

Journal of Steroid Biochemistry and Molecular Biology

Volumn 107, Issue 1-2, 2007, Pages 80-87

  Thomas, James L ^a   Huether, Robert ^b,c   Mack, Vance L ^a   Scaccia, Launa A ^a   Stoner, Ryan C ^a   Duax, William L ^b,c  

^a MERCER UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b HAUPTMAN WOODWARD MEDICAL RESEARCH INSTITUTE   (United States)

^c UNIVERSITY AT BUFFALO   (United States)

Author keywords

3 Hydroxysteroid dehydrogenase; Short chain oxidoreductase; Structure based mutagenesis; Structure function relationship

Indexed keywords

3(OR 17)BETA HYDROXYSTEROID DEHYDROGENASE; 3BETA HYDROXYSTEROID DEHYDROGENASE TYPE 1; 3BETA HYDROXYSTEROID DEHYDROGENASE TYPE 2; CYSTEINE; ISOENZYME; LIGAND; MERCAPTOETHANOL; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME PURIFICATION; ENZYME SUBSTRATE COMPLEX; HUMAN; MICHAELIS CONSTANT; POLYACRYLAMIDE GEL ELECTROPHORESIS; PREDICTION; PROTEIN DOMAIN; REACTION ANALYSIS; SEQUENCE ANALYSIS; WESTERN BLOTTING;

3-HYDROXYSTEROID DEHYDROGENASES; BINDING SITES; COENZYMES; CYSTEINE; HUMANS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY;

EID: 34548382570     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsbmb.2007.02.003     Document Type: Article

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