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http://purl.uniprot.org/citations/22564006http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22564006http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22564006http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/22564006http://www.w3.org/2000/01/rdf-schema#comment"The sequential activities of PhnY, an α-ketoglutarate/Fe(II)-dependent dioxygenase, and PhnZ, a Fe(II)-dependent enzyme of the histidine-aspartate motif hydrolase family, cleave the carbon-phosphorus bond of the organophosphonate natural product 2-aminoethylphosphonic acid. PhnY adds a hydroxyl group to the α-carbon, yielding 2-amino-1-hydroxyethylphosphonic acid, which is oxidatively converted by PhnZ to inorganic phosphate and glycine. The PhnZ reaction represents a new enzyme mechanism for metabolic cleavage of a carbon-phosphorus bond."xsd:string
http://purl.uniprot.org/citations/22564006http://purl.org/dc/terms/identifier"doi:10.1021/ja302072f"xsd:string
http://purl.uniprot.org/citations/22564006http://purl.org/dc/terms/identifier"doi:10.1021/ja302072f"xsd:string
http://purl.uniprot.org/citations/22564006http://purl.uniprot.org/core/author"DeLong E.F."xsd:string
http://purl.uniprot.org/citations/22564006http://purl.uniprot.org/core/author"DeLong E.F."xsd:string
http://purl.uniprot.org/citations/22564006http://purl.uniprot.org/core/author"Hove-Jensen B."xsd:string
http://purl.uniprot.org/citations/22564006http://purl.uniprot.org/core/author"Hove-Jensen B."xsd:string
http://purl.uniprot.org/citations/22564006http://purl.uniprot.org/core/author"Martinez A."xsd:string
http://purl.uniprot.org/citations/22564006http://purl.uniprot.org/core/author"Martinez A."xsd:string
http://purl.uniprot.org/citations/22564006http://purl.uniprot.org/core/author"McSorley F.R."xsd:string
http://purl.uniprot.org/citations/22564006http://purl.uniprot.org/core/author"McSorley F.R."xsd:string
http://purl.uniprot.org/citations/22564006http://purl.uniprot.org/core/author"Wyatt P.B."xsd:string
http://purl.uniprot.org/citations/22564006http://purl.uniprot.org/core/author"Wyatt P.B."xsd:string
http://purl.uniprot.org/citations/22564006http://purl.uniprot.org/core/author"Zechel D.L."xsd:string
http://purl.uniprot.org/citations/22564006http://purl.uniprot.org/core/author"Zechel D.L."xsd:string
http://purl.uniprot.org/citations/22564006http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22564006http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22564006http://purl.uniprot.org/core/name"J. Am. Chem. Soc."xsd:string
http://purl.uniprot.org/citations/22564006http://purl.uniprot.org/core/name"J. Am. Chem. Soc."xsd:string
http://purl.uniprot.org/citations/22564006http://purl.uniprot.org/core/pages"8364-8367"xsd:string
http://purl.uniprot.org/citations/22564006http://purl.uniprot.org/core/pages"8364-8367"xsd:string
http://purl.uniprot.org/citations/22564006http://purl.uniprot.org/core/title"PhnY and PhnZ comprise a new oxidative pathway for enzymatic cleavage of a carbon-phosphorus bond."xsd:string