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http://purl.uniprot.org/citations/9047371http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9047371http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9047371http://www.w3.org/2000/01/rdf-schema#comment"We describe here a sub-family of enzymes related both structurally and functionally to N-acetylneuraminate lyase. Two members of this family (N-acetylneuraminate lyase and dihydrodipicolinate synthase) have known three-dimensional structures and we now proceed to show their structural and functional relationship to two further proteins, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase and D-4-deoxy-5-oxoglucarate dehydratase. These enzymes are all thought to involve intermediate Schiff-base formation with their respective substrates. In order to understand the nature of this intermediate, we have determined the three-dimensional structure of N-acetylneuraminate lyase in complex with hydroxypyruvate (a product analogue) and in complex with one of its products (pyruvate). From these structures we deduce the presence of a closely similar Schiff-base forming motif in all members of the N-acetylneuraminate lyase sub-family. A fifth protein, MosA, is also confirmed to be a member of the sub-family although the involvement of an intermediate Schiff-base in its proposed reaction is unclear."xsd:string
http://purl.uniprot.org/citations/9047371http://purl.org/dc/terms/identifier"doi:10.1006/jmbi.1996.0769"xsd:string
http://purl.uniprot.org/citations/9047371http://purl.org/dc/terms/identifier"doi:10.1006/jmbi.1996.0769"xsd:string
http://purl.uniprot.org/citations/9047371http://purl.uniprot.org/core/author"Lawrence M.C."xsd:string
http://purl.uniprot.org/citations/9047371http://purl.uniprot.org/core/author"Lawrence M.C."xsd:string
http://purl.uniprot.org/citations/9047371http://purl.uniprot.org/core/author"Smith B.J."xsd:string
http://purl.uniprot.org/citations/9047371http://purl.uniprot.org/core/author"Smith B.J."xsd:string
http://purl.uniprot.org/citations/9047371http://purl.uniprot.org/core/author"Hall N.E."xsd:string
http://purl.uniprot.org/citations/9047371http://purl.uniprot.org/core/author"Hall N.E."xsd:string
http://purl.uniprot.org/citations/9047371http://purl.uniprot.org/core/author"Pilling P.A."xsd:string
http://purl.uniprot.org/citations/9047371http://purl.uniprot.org/core/author"Pilling P.A."xsd:string
http://purl.uniprot.org/citations/9047371http://purl.uniprot.org/core/author"Barbosa J.A.R.G."xsd:string
http://purl.uniprot.org/citations/9047371http://purl.uniprot.org/core/author"Barbosa J.A.R.G."xsd:string
http://purl.uniprot.org/citations/9047371http://purl.uniprot.org/core/author"Marcuccio S.M."xsd:string
http://purl.uniprot.org/citations/9047371http://purl.uniprot.org/core/author"Marcuccio S.M."xsd:string
http://purl.uniprot.org/citations/9047371http://purl.uniprot.org/core/author"Ooi H.C."xsd:string
http://purl.uniprot.org/citations/9047371http://purl.uniprot.org/core/author"Ooi H.C."xsd:string
http://purl.uniprot.org/citations/9047371http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9047371http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9047371http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/9047371http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/9047371http://purl.uniprot.org/core/pages"381-399"xsd:string
http://purl.uniprot.org/citations/9047371http://purl.uniprot.org/core/pages"381-399"xsd:string