Butane and propane oxidation by engineered cytochrome P450cam

The haem monooxygenase cytochrome P450cam has been engineered to oxidise the gaseous alkanes butane and propane to butan-2-ol and propan-2-ol, respectively, by the use of bulky amino acid substitutions to reduce the volume of the substrate pocket and thus improve the enzyme-substrate fit: the F87W/Y...

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Veröffentlicht in:	Chemical communications (Cambridge, England) England), 2002-03 (5), p.490-491
Hauptverfasser:	Bell, Stephen G, Stevenson, Julie-Anne, Boyd, Helen D, Campbell, Sophie, Riddle, Austin D, Orton, Erica L, Wong, Luet-Lok
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites - genetics Butanes - metabolism Butanols Camphor 5-Monooxygenase - genetics Camphor 5-Monooxygenase - metabolism Kinetics Mutagenesis, Site-Directed Oxidation-Reduction Propane - metabolism Propanols Protein Engineering Pseudomonas putida - enzymology
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Beschreibung
Zusammenfassung:	The haem monooxygenase cytochrome P450cam has been engineered to oxidise the gaseous alkanes butane and propane to butan-2-ol and propan-2-ol, respectively, by the use of bulky amino acid substitutions to reduce the volume of the substrate pocket and thus improve the enzyme-substrate fit: the F87W/Y96F/T101L/V247L mutant oxidizes butane with a turnover rate of 750 min-1 and 95% yield based on NADH consumed while the wild-type enzyme has an activity of 0.4 min-1 with 4% yield.
ISSN:	1359-7345 1364-548X
DOI:	10.1039/b110957j