Interactions across the interface contribute the stability of homodimeric 3α-hydroxysteroid dehydrogenase/carbonyl reductase

Archives of Biochemistry and Biophysics

Volumn 490, Issue 1, 2009, Pages 36-41

  Hwang, Chi Ching ^a   Hsu, Chao Nan ^a   Huang, Tzu Jung ^a   Chiou, Shean Jaw ^a   Hong, Yi Ren ^a  

^a KAOHSIUNG MEDICAL UNIVERSITY   (Taiwan)

Author keywords

Catalysis; Conformational stability; Dehydrogenase; Oligomerization; Salt bridge

Indexed keywords

3ALPHA HYDROXYSTEROID DEHYDROGENASE; ALANINE; CARBONYL REDUCTASE; LYSINE; SERINE; UREA;

AMINO ACID SUBSTITUTION; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; DIMERIZATION; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME STABILITY; ESCHERICHIA COLI; GENE MUTATION; HEAT STRESS; MELTING POINT; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; SITE DIRECTED MUTAGENESIS; WILD TYPE;

3-ALPHA-HYDROXYSTEROID DEHYDROGENASE (B-SPECIFIC); ALANINE; AMINO ACID SEQUENCE; CATALYSIS; DIMERIZATION; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME STABILITY; ESCHERICHIA COLI; KINETICS; LYSINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING; SERINE; STRUCTURAL HOMOLOGY, PROTEIN; SUBSTRATE SPECIFICITY; TEMPERATURE; TRANSFORMATION, GENETIC; UREA;

EID: 70349451554     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2009.08.006     Document Type: Article

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