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http://purl.uniprot.org/citations/21216900http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21216900http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21216900http://www.w3.org/2000/01/rdf-schema#comment"Terminal olefins (1-alkenes) are natural products that have important industrial applications as both fuels and chemicals. However, their biosynthesis has been largely unexplored. We describe a group of bacteria, Jeotgalicoccus spp., which synthesize terminal olefins, in particular 18-methyl-1-nonadecene and 17-methyl-1-nonadecene. These olefins are derived from intermediates of fatty acid biosynthesis, and the key enzyme in Jeotgalicoccus sp. ATCC 8456 is a terminal olefin-forming fatty acid decarboxylase. This enzyme, Jeotgalicoccus sp. OleT (OleT(JE)), was identified by purification from cell lysates, and its encoding gene was identified from a draft genome sequence of Jeotgalicoccus sp. ATCC 8456 using reverse genetics. Heterologous expression of the identified gene conferred olefin biosynthesis to Escherichia coli. OleT(JE) is a P450 from the cyp152 family, which includes bacterial fatty acid hydroxylases. Some cyp152 P450 enzymes have the ability to decarboxylate and to hydroxylate fatty acids (in α-and/or β-position), suggesting a common reaction intermediate in their catalytic mechanism and specific structural determinants that favor one reaction over the other. The discovery of these terminal olefin-forming P450 enzymes represents a third biosynthetic pathway (in addition to alkane and long-chain olefin biosynthesis) to convert fatty acid intermediates into hydrocarbons. Olefin-forming fatty acid decarboxylation is a novel reaction that can now be added to the catalytic repertoire of the versatile cytochrome P450 enzyme family."xsd:string
http://purl.uniprot.org/citations/21216900http://purl.org/dc/terms/identifier"doi:10.1128/AEM.02580-10"xsd:string
http://purl.uniprot.org/citations/21216900http://purl.org/dc/terms/identifier"doi:10.1128/aem.02580-10"xsd:string
http://purl.uniprot.org/citations/21216900http://purl.uniprot.org/core/author"Rude M.A."xsd:string
http://purl.uniprot.org/citations/21216900http://purl.uniprot.org/core/author"Rude M.A."xsd:string
http://purl.uniprot.org/citations/21216900http://purl.uniprot.org/core/author"Schirmer A."xsd:string
http://purl.uniprot.org/citations/21216900http://purl.uniprot.org/core/author"Schirmer A."xsd:string
http://purl.uniprot.org/citations/21216900http://purl.uniprot.org/core/author"Alibhai M."xsd:string
http://purl.uniprot.org/citations/21216900http://purl.uniprot.org/core/author"Alibhai M."xsd:string
http://purl.uniprot.org/citations/21216900http://purl.uniprot.org/core/author"Baron T.S."xsd:string
http://purl.uniprot.org/citations/21216900http://purl.uniprot.org/core/author"Baron T.S."xsd:string
http://purl.uniprot.org/citations/21216900http://purl.uniprot.org/core/author"Brubaker S."xsd:string
http://purl.uniprot.org/citations/21216900http://purl.uniprot.org/core/author"Brubaker S."xsd:string
http://purl.uniprot.org/citations/21216900http://purl.uniprot.org/core/author"Del Cardayre S.B."xsd:string
http://purl.uniprot.org/citations/21216900http://purl.uniprot.org/core/author"Del Cardayre S.B."xsd:string
http://purl.uniprot.org/citations/21216900http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21216900http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21216900http://purl.uniprot.org/core/name"Appl. Environ. Microbiol."xsd:string
http://purl.uniprot.org/citations/21216900http://purl.uniprot.org/core/name"Appl Environ Microbiol"xsd:string
http://purl.uniprot.org/citations/21216900http://purl.uniprot.org/core/pages"1718-1727"xsd:string
http://purl.uniprot.org/citations/21216900http://purl.uniprot.org/core/pages"1718-1727"xsd:string
http://purl.uniprot.org/citations/21216900http://purl.uniprot.org/core/title"Terminal olefin (1-alkene) biosynthesis by a novel p450 fatty acid decarboxylase from Jeotgalicoccus species."xsd:string
http://purl.uniprot.org/citations/21216900http://purl.uniprot.org/core/title"Terminal olefin (1-alkene) biosynthesis by a novel p450 fatty acid decarboxylase from Jeotgalicoccus species."xsd:string