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http://purl.uniprot.org/citations/18275154http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18275154http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18275154http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/18275154http://www.w3.org/2000/01/rdf-schema#comment"Legionaminic acid is a nine-carbon alpha-keto acid that is similar in structure to other members of the sialic acid family that includes neuraminic acid and pseudaminic acid. It is found as a component of the lipopolysaccharide in several bacterial species and is perhaps best known for its presence in the O-antigen of the causative agent of Legionnaires' disease, Legionella pneumophila. In this work, the enzymes responsible for the biosynthesis and activation of N, N'-diacetyllegionaminic acid are identified for the first time. A cluster of three L. pneumophila genes bearing homology to known sialic acid biosynthetic genes ( neuA,B,C) were cloned and overexpressed in Escherichia coli. The NeuC homologue was found to be a hydrolyzing UDP-N, N'-diacetylbacillosamine 2-epimerase that converts UDP-N, N'-diacetylbacillosamine into 2,4-diacetamido-2,4,6-trideoxymannose and UDP. Stereochemical and isotopic labeling studies showed that the enzyme utilizes a mechanism involving an initial anti elimination of UDP to form a glycal intermediate and a subsequent syn addition of water to generate product. This is similar to the hydrolyzing UDP-N-acetylglucosamine 2-epimerase (NeuC) of sialic acid biosynthesis, but the L. pneumophila enzyme would not accept UDP-GlcNAc as an alternate substrate. The NeuB homologue was found to be a N, N'-diacetyllegionaminic acid synthase that condenses 2,4-diacetamido-2,4,6-trideoxymannose with phosphoenolpyruvate (PEP), although the in vitro activity of the recombinant enzyme (isolated as a MalE fusion protein) was very low. The synthase activity was dependent on the presence of a divalent metal ion, and the reaction proceeded via a C-O bond cleavage process, similar to the reactions catalyzed by the sialic acid and pseudaminic acid synthases. Finally, the NeuA homologue was shown to possess the CMP-N, N'-diacetyllegionaminic acid synthetase activity that generates the activated form of legionaminic acid used in lipopolysaccharide biosynthesis. Together, the three enzymes constitute a pathway that converts a UDP-linked bacillosamine derivative into a CMP-linked legionaminic acid derivative."xsd:string
http://purl.uniprot.org/citations/18275154http://purl.org/dc/terms/identifier"doi:10.1021/bi702364s"xsd:string
http://purl.uniprot.org/citations/18275154http://purl.org/dc/terms/identifier"doi:10.1021/bi702364s"xsd:string
http://purl.uniprot.org/citations/18275154http://purl.uniprot.org/core/author"Young N.M."xsd:string
http://purl.uniprot.org/citations/18275154http://purl.uniprot.org/core/author"Young N.M."xsd:string
http://purl.uniprot.org/citations/18275154http://purl.uniprot.org/core/author"Tanner M.E."xsd:string
http://purl.uniprot.org/citations/18275154http://purl.uniprot.org/core/author"Tanner M.E."xsd:string
http://purl.uniprot.org/citations/18275154http://purl.uniprot.org/core/author"Watson D.C."xsd:string
http://purl.uniprot.org/citations/18275154http://purl.uniprot.org/core/author"Watson D.C."xsd:string
http://purl.uniprot.org/citations/18275154http://purl.uniprot.org/core/author"Glaze P.A."xsd:string
http://purl.uniprot.org/citations/18275154http://purl.uniprot.org/core/author"Glaze P.A."xsd:string
http://purl.uniprot.org/citations/18275154http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18275154http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18275154http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/18275154http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/18275154http://purl.uniprot.org/core/pages"3272-3282"xsd:string
http://purl.uniprot.org/citations/18275154http://purl.uniprot.org/core/pages"3272-3282"xsd:string
http://purl.uniprot.org/citations/18275154http://purl.uniprot.org/core/title"Biosynthesis of CMP-N,N'-diacetyllegionaminic acid from UDP-N,N'-diacetylbacillosamine in Legionella pneumophila."xsd:string
http://purl.uniprot.org/citations/18275154http://purl.uniprot.org/core/title"Biosynthesis of CMP-N,N'-diacetyllegionaminic acid from UDP-N,N'-diacetylbacillosamine in Legionella pneumophila."xsd:string
http://purl.uniprot.org/citations/18275154http://purl.uniprot.org/core/volume"47"xsd:string
http://purl.uniprot.org/citations/18275154http://purl.uniprot.org/core/volume"47"xsd:string
http://purl.uniprot.org/citations/18275154http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18275154
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