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http://purl.uniprot.org/citations/8227039http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8227039http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8227039http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/8227039http://www.w3.org/2000/01/rdf-schema#comment"The 5-methylthio-D-ribose moiety of 5'-(methylthio)-adenosine is converted to methionine in a wide variety of organisms. 2,3-Diketo-5-methylthio-1-phosphopentane is an advanced intermediate in the methionine recycling pathway present in the Gram-negative bacterium Klebsiella pneumoniae. This unusual metabolite is oxidatively cleaved to yield formate (from C-1), 2-keto-4-methylthiobutyrate (the transamination product of methionine), and 3-methylthiopropionate. To further characterize this oxidative conversion, the desthio analog of the naturally occurring diketone, namely 2,3-diketo-1-phosphohexane I, was synthesized. If the metabolism of I is analogous to that of 2,3-diketo-5-methylthio-1-phosphopentane it should be converted to formate, 2-ketopentanoate, and butyrate. An enzyme (E-1), which mediates the oxidative conversion of I to formate and 2-ketopentanoate, was isolated from extracts of K. pneumoniae. E-1 was purified 100-fold to homogeneity in 10% yield. The native enzyme is a monomeric protein of M(r) 27,000. The activity of E-1 requires magnesium ion as a cofactor. No other prosthetic groups were detected. Incubation of the enzyme with I, under anaerobic conditions, led to the discovery of two intermediates. These species have been identified by 1H and 13C NMR, UV-visible spectroscopy, and model chemistry studies as 2-hydroxy-3-keto-1-phospho-1-hexene II, generated by enolization of I; and 1,2-dihydroxy-3-keto-1-hexene III, generated by enzymatic dephosphorylation of II. Intermediates II and III are released from the active site of the enzyme; III accumulates under anaerobic conditions. Under aerobic conditions, III is non-enzymically oxidized to 2-ketopentanoate, formate, and other products. Compound II was also generated by heating I at pH 7.5 for 7 min. Action of alkaline phosphatase on II produces III."xsd:string
http://purl.uniprot.org/citations/8227039http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(19)74533-5"xsd:string
http://purl.uniprot.org/citations/8227039http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(19)74533-5"xsd:string
http://purl.uniprot.org/citations/8227039http://purl.uniprot.org/core/author"Myers R.W."xsd:string
http://purl.uniprot.org/citations/8227039http://purl.uniprot.org/core/author"Myers R.W."xsd:string
http://purl.uniprot.org/citations/8227039http://purl.uniprot.org/core/author"Abeles R.H."xsd:string
http://purl.uniprot.org/citations/8227039http://purl.uniprot.org/core/author"Abeles R.H."xsd:string
http://purl.uniprot.org/citations/8227039http://purl.uniprot.org/core/author"Fish S."xsd:string
http://purl.uniprot.org/citations/8227039http://purl.uniprot.org/core/author"Fish S."xsd:string
http://purl.uniprot.org/citations/8227039http://purl.uniprot.org/core/author"Wray J.W."xsd:string
http://purl.uniprot.org/citations/8227039http://purl.uniprot.org/core/author"Wray J.W."xsd:string
http://purl.uniprot.org/citations/8227039http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8227039http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8227039http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8227039http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8227039http://purl.uniprot.org/core/pages"24785-24791"xsd:string
http://purl.uniprot.org/citations/8227039http://purl.uniprot.org/core/pages"24785-24791"xsd:string
http://purl.uniprot.org/citations/8227039http://purl.uniprot.org/core/title"Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae."xsd:string
http://purl.uniprot.org/citations/8227039http://purl.uniprot.org/core/title"Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae."xsd:string
http://purl.uniprot.org/citations/8227039http://purl.uniprot.org/core/volume"268"xsd:string
http://purl.uniprot.org/citations/8227039http://purl.uniprot.org/core/volume"268"xsd:string
http://purl.uniprot.org/citations/8227039http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8227039
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