Functional interaction between amino-acid residues 242 and 290 in cytochromes P-450 2B1 and 2B11

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1338, Issue 2, 1997, Pages 259-266

  Harlow, Greg R ^a   He, You Ai ^a   Halpert, James R ^a  

^a UNIVERSITY OF ARIZONA   (United States)

Author keywords

Cytochrome P 450 mutant; E. coli; Expression; Structure function relationship

Indexed keywords

AMINO ACID; CYTOCHROME P450 ISOENZYME;

ARTICLE; ESCHERICHIA COLI; MUTAGENESIS; MUTANT; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

ANDROSTENEDIONE; ANIMALS; ARYL HYDROCARBON HYDROXYLASES; ASPARTIC ACID; CARBON MONOXIDE; CYTOCHROME P-450 CYP2B1; CYTOCHROME P-450 ENZYME SYSTEM; DOGS; HUMANS; LYSINE; MICE; MUTAGENESIS, SITE-DIRECTED; PROTEIN FOLDING; RABBITS; RATS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SPECTRUM ANALYSIS; STEROID HYDROXYLASES; STRUCTURE-ACTIVITY RELATIONSHIP;

CANIS FAMILIARIS; ESCHERICHIA COLI;

EID: 0030915458     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(96)00209-9     Document Type: Article

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