The functions of key residues in the inhibitor, substrate and cofactor sites of human 3β-hydroxysteroid dehydrogenase type 1 are validated by mutagenesis

Journal of Steroid Biochemistry and Molecular Biology

Volumn 120, Issue 4-5, 2010, Pages 192-199

  Thomas, James L ^a   Mack, Vance L ^a   Sun, Jingping ^a   Terrell, J Ross ^b   Bucholtz, Kevin M ^b  

^a MERCER UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b MERCER UNIVERSITY   (United States)

Author keywords

3 Hydroxysteroid dehydrogenase; Mutagenesis; Short chain dehydrogenase reductase; Structure function relationship

Indexed keywords

3(OR 17)BETA HYDROXYSTEROID DEHYDROGENASE; 3(OR 17)BETA HYDROXYSTEROID DEHYDROGENASE 1; 3(OR 17)BETA HYDROXYSTEROID DEHYDROGENASE 2; PRASTERONE; TRILOSTANE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; COMPETITIVE INHIBITION; CONTROLLED STUDY; HUMAN; MICHAELIS MENTEN KINETICS; MOLECULAR DOCKING; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

3-HYDROXYSTEROID DEHYDROGENASES; AMINO ACIDS; BINDING SITES; BREAST NEOPLASMS; DEHYDROEPIANDROSTERONE; DIHYDROTESTOSTERONE; FEMALE; HUMANS; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY;

EID: 77953615777     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsbmb.2010.04.015     Document Type: Article

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