Evolved CYP102A1 (P450BM3) variants oxidise a range of non-natural substrates and offer new selectivity options.
The evolution of CYP102A1 variants with enhanced activity and altered specificity characteristics.
Whitehouse
Christopher J C
CJ
Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, UK OX1 3QR.
Bell
Stephen G
SG
Tufton
Henry G
HG
Kenny
Richard J P
RJ
Ogilvie
Lydia C I
LC
Wong
Luet-Lok
LL
D001410:Bacillus megaterium / Q000201:enzymology; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D001555:Benzene Derivatives / Q000737:chemistry; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D019020:Directed Molecular Evolution; D004789:Enzyme Activation; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D015394:Molecular Structure; D016296:Mutagenesis; D009251:NADPH-Ferrihemoprotein Reductase; D009281:Naphthalenes / Q000737:chemistry; D010084:Oxidation-Reduction; D013379:Substrate Specificity; D013997:Time Factors
D001426:Bacterial Proteins; D001555:Benzene Derivatives; D009281:Naphthalenes; C024268:n-propylbenzene; C031721:naphthalene; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D009251:NADPH-Ferrihemoprotein Reductase; C052423:flavocytochrome P450 BM3 monoxygenases