Engineering microsomal cytochrome P450 2C5 to be a soluble, monomeric enzyme: Mutations that alter aggregation, phospholipid dependence of catalysis, and membrane binding

Journal of Biological Chemistry

Volumn 275, Issue 4, 2000, Pages 2545-2553

  Cosme, Jose ^a   Johnson, Eric F ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME P450; CYTOCHROME P450 ISOENZYME; DIMER; PHOSPHOLIPID; TETRAMER;

AMINO ACID SUBSTITUTION; ARTICLE; BIOENGINEERING; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME BINDING; GENE DELETION; GENE MUTATION; MEMBRANE BINDING; MEMBRANE VESICLE; MICROSOME; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DOMAIN; PROTEIN INTERACTION;

AMINO ACID SEQUENCE; CATALYSIS; CELL MEMBRANE; CYTOCHROME P-450 ENZYME SYSTEM; ESCHERICHIA COLI; HYDROXYLATION; LIPOSOMES; MICROSOMES; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHOSPHATIDYLCHOLINES; PROGESTERONE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN ENGINEERING; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SOLUBILITY; STEROID 21-HYDROXYLASE; SUBCELLULAR FRACTIONS;

EID: 0034723195     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.275.4.2545     Document Type: Article

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