A single mutation in cytochrome P450 BM3 induces the conformational rearrangement seen upon substrate binding in the wild-type enzyme

Journal of Biological Chemistry

Volumn 279, Issue 22, 2004, Pages 23287-23293

  Joyce, M Gordon ^a   Girvan, Hazel M ^a   Munro, Andrew W ^a   Leys, David ^a  

^a UNIVERSITY OF LEICESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CRYSTAL STRUCTURE; ENZYMES; FATTY ACIDS; MUTAGENS;

HOMOLOGY; SUBSTRATE BINDING;

BIOCHEMISTRY;

CYTOCHROME P450; FATTY ACID; FLAVOCYTOCHROME P450 BM3; GLUTAMIC ACID; HEME; MUTANT PROTEIN; OXIDOREDUCTASE; PALMITOLEIC ACID; PROTEIN A264E; STRUCTURAL PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ELECTRON TRANSPORT; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; GENE MUTATION; GENE REARRANGEMENT; LIGAND BINDING; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN DOMAIN; RECEPTOR BINDING; WILD TYPE;

BACTERIAL PROTEINS; BINDING SITES; CYTOCHROME P-450 ENZYME SYSTEM; HEME; MIXED FUNCTION OXYGENASES; MODELS, MOLECULAR; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY;

EUKARYOTA;

EID: 2542439885     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M401717200     Document Type: Article

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