A single active-site mutation of P450BM-3 dramatically enhances substrate binding and rate of product formation

Biochemistry

Volumn 50, Issue 39, 2011, Pages 8333-8341

  Haines, Donovan C ^a   Hegde, Amita ^b   Chen, Baozhi ^b   Zhao, Weiqiang ^c   Bondlela, Muralidhar ^b   Humphreys, John M ^b   Mullin, David A ^d   Tomchick, Diana R ^b   MacHius, Mischa ^b   Peterson, Julian A ^b  

^a SAM HOUSTON STATE UNIVERSITY   (United States)

^b UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^c THE OHIO STATE UNIVERSITY WEXNER MEDICAL CENTER   (United States)

^d Tulane University   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BINDING AFFINITIES; CATALYTIC MECHANISMS; CYTOCHROMES P450; DRUG-METABOLIZING ENZYMES; E. COLI; METHYL GROUP; PRODUCT FORMATION; SITE-SPECIFIC MUTAGENESIS; STEREO-SELECTIVE; STRUCTURAL FEATURE; SUBSTRATE AFFINITY; SUBSTRATE BINDING; SUBSTRATE RECOGNITION; SUBSTRATE-BOUND; TURNOVER NUMBER; WILD TYPES; WILD-TYPE ENZYMES;

AMINO ACIDS; BINDING ENERGY; CRYSTAL STRUCTURE; ENZYMES; ESCHERICHIA COLI; FATTY ACIDS; FUNCTIONAL GROUPS;

SUBSTRATES;

ALANINE; CYTOCHROME P450; VALINE;

ARTICLE; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME METABOLISM; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; GENE MUTATION; HYDROXYLATION; MOLECULAR MECHANICS; MOLECULAR MODEL; MOLECULAR RECOGNITION; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN LOCALIZATION; STEREOCHEMISTRY; WILD TYPE;

ALANINE; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; CYTOCHROME P-450 ENZYME SYSTEM; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NADPH-FERRIHEMOPROTEIN REDUCTASE; SUBSTRATE SPECIFICITY; VALINE;

EID: 80053427540     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201099j     Document Type: Article

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