Key mutations alter the cytochrome P450 BM3 conformational landscape and remove inherent substrate bias

Journal of Biological Chemistry

Volumn 288, Issue 35, 2013, Pages 25387-25399

  Butler, Christopher F ^a   Peet, Caroline ^b   Mason, Amy E ^a   Voice, Michael W ^b   Leys, David ^a   Munro, Andrew W ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

^b Dundee DD2 1NH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BIOTECHNOLOGICAL POTENTIALS; CONFORMATIONAL STATE; CYTOCHROME P450 BM3; ENERGETIC BARRIERS; HIGH ACTIVITY; SUBSTRATE BIAS; SUBSTRATE-BOUND;

ENZYME ACTIVITY;

SUBSTRATES;

CYTOCHROME P450 2C19; CYTOCHROME P450 BM3; OMEPRAZOLE;

ARTICLE; BACILLUS MEGATERIUM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DRUG STRUCTURE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; GENE MUTATION; HETERONUCLEAR MULTIPLE BOND CORRELATION; HETERONUCLEAR MULTIPLE QUANTUM COHERENCE; HYDROXYLATION; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; MOLECULAR RECOGNITION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL;

CALORIMETRY; CONFORMATIONAL DESTABILIZATION; CRYSTAL STRUCTURE; CYTOCHROME P450; DRUG METABOLISM; ENZYME CATALYSIS; HYDROXYLASE; OMEPRAZOLE; P450 BM3; SITE-DIRECTED MUTAGENESIS;

ARYL HYDROCARBON HYDROXYLASES; BACILLUS MEGATERIUM; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; CYTOCHROME P-450 ENZYME SYSTEM; HUMANS; HYDROXYLATION; MUTATION; NADPH-FERRIHEMOPROTEIN REDUCTASE; OMEPRAZOLE; OXIDATION-REDUCTION; PROTEIN STRUCTURE, TERTIARY; PROTON PUMP INHIBITORS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84883401015     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.479717     Document Type: Article

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