Serine 124 completes the Tyr, Lys and Ser triad responsible for the catalysis of human type 1 3β-hydroxysteroid dehydrogenase

Journal of Molecular Endocrinology

Volumn 33, Issue 1, 2004, Pages 253-261

  Thomas, James L ^d   Duax, W L ^a,b   Addlagatta, A ^b,c   Scaccia, L A ^d   Frizzell, K A ^d   Carloni, S B ^d  

^a Hauptman Woodward Medical Institute   (United States)

^b UNIVERSITY AT BUFFALO   (United States)

^c UNIVERSITY OF OREGON   (United States)

^d MERCER UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

17 HYDROXYPREGNENOLONE; 3(OR 17)BETA HYDROXYSTEROID DEHYDROGENASE; ALDOSTERONE; ANDROSTENEDIONE; ESTRADIOL; HYDROCORTISONE; HYDROXYL GROUP; LYSINE; PRASTERONE; PREGNENOLONE; PROGESTERONE; SERINE; STEROID HORMONE; TESTOSTERONE; TYROSINE;

ACCURACY; ARTICLE; BACULOVIRUS; BREAST TUMOR; CANCER INHIBITION; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; ENZYME MECHANISM; ENZYME PURIFICATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; HORMONE SENSITIVITY; INSECT CELL; LABOR; PH; POLYMERASE CHAIN REACTION; PREDICTION; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; STEROIDOGENESIS; STRUCTURE ACTIVITY RELATION; VALIDATION PROCESS; WILD TYPE;

3-HYDROXYSTEROID DEHYDROGENASES; AMINO ACID SEQUENCE; BASE SEQUENCE; CATALYSIS; CATALYTIC DOMAIN; DNA PRIMERS; HUMANS; KINETICS; LYSINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; POLYMERASE CHAIN REACTION; SERINE; TYROSINE;

EID: 4444293344     PISSN: 09525041     EISSN: None     Source Type: Journal    
DOI: 10.1677/jme.0.0330253     Document Type: Article

References (25)

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