Rational proteomics V: Structure-based mutagenesis has revealed key residues responsible for substrate recognition and catalysis by the dehydrogenase and isomerase activities in human 3β-hydroxysteroid dehydrogenase/isomerase type 1

Journal of Steroid Biochemistry and Molecular Biology

Volumn 101, Issue 1, 2006, Pages 50-60

  Pletnev, Vladimir Z ^a,b   Thomas, James L ^c   Rhaney, Felicia L ^c   Holt, Lynley S ^c   Scaccia, Launa A ^c   Umland, Timothy C ^a   Duax, William L ^a  

^a UNIVERSITY AT BUFFALO   (United States)

^b SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

^c MERCER UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

3 Hydroxysteroid dehydrogenase; 3D model structure; Bioinformatics; Rational proteomics; Short chain oxidoreductase; Structure based mutagenesis; Structure function relationship

Indexed keywords

3(OR 17)BETA HYDROXYSTEROID DEHYDROGENASE; ANDROSTENEDIONE; ISOMERASE; MONOMER; MUTANT PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; TESTOSTERONE 17BETA DEHYDROGENASE; URIDINE DIPHOSPHATE GLUCOSE 4 EPIMERASE;

ARTICLE; CATALYSIS; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; ISOMERIZATION; MUTAGENESIS; PROTEOMICS; STREPTOCOCCUS SUIS; STRUCTURE ANALYSIS; X RAY ANALYSIS;

AMINO ACID SEQUENCE; BASE SEQUENCE; CATALYSIS; DNA PRIMERS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIENZYME COMPLEXES; MUTAGENESIS, SITE-DIRECTED; PROGESTERONE REDUCTASE; PROTEOMICS; SEQUENCE HOMOLOGY, AMINO ACID; STEROID ISOMERASES; SUBSTRATE SPECIFICITY;

MAMMALIA; STREPTOCOCCUS SUIS;

EID: 33748060523     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsbmb.2006.06.004     Document Type: Article

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