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http://purl.uniprot.org/citations/30810303http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30810303http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30810303http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/30810303http://www.w3.org/2000/01/rdf-schema#comment"Methylphosphonic acid is synthesized by marine bacteria and is a prominent component of dissolved organic phosphorus. Consequently, methylphosphonic acid also serves as a source of inorganic phosphate (Pi) for marine bacteria that are starved of this nutrient. Conversion of methylphosphonic acid into Pi is currently only known to occur through the carbon-phosphorus lyase pathway, yielding methane as a byproduct. In this work, we describe an oxidative pathway for the catabolism of methylphosphonic acid in Gimesia maris DSM8797. G. maris can use methylphosphonic acid as Pi sources despite lacking a phn operon encoding a carbon-phosphorus lyase pathway. Instead, the genome contains a locus encoding homologues of the non-heme Fe(II) dependent oxygenases HF130PhnY* and HF130PhnZ, which were previously shown to convert 2-aminoethylphosphonic acid into glycine and Pi. GmPhnY* and GmPhnZ1 were produced in E. coli and purified for characterization in vitro. The substrate specificities of the enzymes were evaluated with a panel of synthetic phosphonates. Via 31P NMR spectroscopy, it is demonstrated that the GmPhnY* converts methylphosphonic acid to hydroxymethylphosphonic acid, which in turn is oxidized by GmPhnZ1 to produce formic acid and Pi. In contrast, 2-aminoethylphosphonic acid is not a substrate for GmPhnY* and is therefore not a substrate for this pathway. These results thus reveal a new metabolic fate for methylphosphonic acid."xsd:string
http://purl.uniprot.org/citations/30810303http://purl.org/dc/terms/identifier"doi:10.1021/acschembio.9b00024"xsd:string
http://purl.uniprot.org/citations/30810303http://purl.org/dc/terms/identifier"doi:10.1021/acschembio.9b00024"xsd:string
http://purl.uniprot.org/citations/30810303http://purl.uniprot.org/core/author"Hammerschmidt F."xsd:string
http://purl.uniprot.org/citations/30810303http://purl.uniprot.org/core/author"Hammerschmidt F."xsd:string
http://purl.uniprot.org/citations/30810303http://purl.uniprot.org/core/author"Zechel D.L."xsd:string
http://purl.uniprot.org/citations/30810303http://purl.uniprot.org/core/author"Zechel D.L."xsd:string
http://purl.uniprot.org/citations/30810303http://purl.uniprot.org/core/author"Gama S.R."xsd:string
http://purl.uniprot.org/citations/30810303http://purl.uniprot.org/core/author"Gama S.R."xsd:string
http://purl.uniprot.org/citations/30810303http://purl.uniprot.org/core/author"Hupp K."xsd:string
http://purl.uniprot.org/citations/30810303http://purl.uniprot.org/core/author"Hupp K."xsd:string
http://purl.uniprot.org/citations/30810303http://purl.uniprot.org/core/author"Kalina T."xsd:string
http://purl.uniprot.org/citations/30810303http://purl.uniprot.org/core/author"Kalina T."xsd:string
http://purl.uniprot.org/citations/30810303http://purl.uniprot.org/core/author"Pallitsch K."xsd:string
http://purl.uniprot.org/citations/30810303http://purl.uniprot.org/core/author"Pallitsch K."xsd:string
http://purl.uniprot.org/citations/30810303http://purl.uniprot.org/core/author"Vogt M."xsd:string
http://purl.uniprot.org/citations/30810303http://purl.uniprot.org/core/author"Vogt M."xsd:string
http://purl.uniprot.org/citations/30810303http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/30810303http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/30810303http://purl.uniprot.org/core/name"ACS Chem. Biol."xsd:string
http://purl.uniprot.org/citations/30810303http://purl.uniprot.org/core/name"ACS Chem. Biol."xsd:string
http://purl.uniprot.org/citations/30810303http://purl.uniprot.org/core/pages"735-741"xsd:string