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Titolo:
Directed evolution of a cytochrome P450 monooxygenase for alkane oxidation
Autore:
Farinas, ET; Schwaneberg, U; Glieder, A; Arnold, FH;
Indirizzi:
CALTECH, Div Chem & Chem Engn 210 41, Pasadena, CA 91125 USA CALTECH Pasadena CA USA 91125 & Chem Engn 210 41, Pasadena, CA 91125 USA
Titolo Testata:
ADVANCED SYNTHESIS & CATALYSIS
fascicolo: 6-7, volume: 343, anno: 2001,
pagine: 601 - 606
SICI:
1615-4150(200108)343:6-7<601:DEOACP>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
FATTY-ACID MONOOXYGENATION; BACILLUS-MEGATERIUM; SUBSTRATE-SPECIFICITY; ESCHERICHIA-COLI; HYDROXYLATION; ENZYME; EXPRESSION; OMEGA-2; BM-3;
Keywords:
alkanes; cytochrome P450BM-3; enzyme catalysis; enzyme engineering; in vitro evolution;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Arnold, FH CALTECH, Div Chem & Chem Engn 210 41, Pasadena, CA 91125 USA CALTECH Pasadena CA USA 91125 n 210 41, Pasadena, CA 91125 USA
Citazione:
E.T. Farinas et al., "Directed evolution of a cytochrome P450 monooxygenase for alkane oxidation", ADV SYNTH C, 343(6-7), 2001, pp. 601-606

Abstract

Cytochrome P450 monooxygenase BM-3 (EC 1.14.14.1) hydroxylates fatty acidswith chain lengths between C-12 and C-18. It is also known to oxidize the corresponding alcohols and amides. However, it is not known to oxidize alkanes. Here we report that P450 BM-3 oxidizes octane, which is four carbons shorter and lacks the carboxylate functionality of the shortest fatty acid P450 BM-3 is known to accept, to 4-octanol, 3-octanol, 2-octanol, 4-octanone, and 3-octanone. The rate is much lower than for oxidation of the preferred fatty acid substrates. In an effort to explore the plasticity and mechanisms of substrate recognition in this powerful biocatalyst, we are using directed evolution - random mutagenesis, recombination, and screening - to improve its activity towards saturated hydrocarbons. A spectrophotometric assay has been validated for high throughput screening, and two generations of laboratory evolution have yielded variants displaying up to five times the specific activity of wild-type P450 BM-3.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 18:11:07