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http://purl.uniprot.org/citations/17804405http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17804405http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17804405http://www.w3.org/2000/01/rdf-schema#comment"The molecular identity of mammalian phosphopentomutase has not yet been established unequivocally. That of glucose-1,6-bisphosphate synthase, the enzyme that synthesizes a cofactor for phosphomutases and putative regulator of glycolysis, is completely unknown. In the present work, we have purified phosphopentomutase from human erythrocytes and found it to copurify with a 68-kDa polypeptide that was identified by mass spectrometry as phosphoglucomutase 2 (PGM2), a protein of the alpha-d-phosphohexomutase family and sharing about 20% identity with mammalian phosphoglucomutase 1. Data base searches indicated that vertebrate genomes contained, in addition to PGM2, a homologue (PGM2L1, for PGM2-like 1) sharing about 60% sequence identity with this protein. Both PGM2 and PGM2L1 were overexpressed in Escherichia coli, purified, and their properties were studied. Using catalytic efficiency as a criterion, PGM2 acted more than 10-fold better as a phosphopentomutase (both on deoxyribose 1-phosphate and on ribose 1-phosphate) than as a phosphoglucomutase. PGM2L1 showed only low (<5%) phosphopentomutase and phosphoglucomutase activities compared with PGM2, but was about 5-20-fold better than the latter enzyme in catalyzing the 1,3-bisphosphoglycerate-dependent synthesis of glucose 1,6-bisphosphate and other aldose-bisphosphates. Furthermore, quantitative real-time PCR analysis indicated that PGM2L1 was mainly expressed in brain where glucose-1,6-bisphosphate synthase activity was previously shown to be particularly high. We conclude that mammalian phosphopentomutase and glucose-1,6-bisphosphate synthase correspond to two closely related proteins, PGM2 and PGM2L1, encoded by two genes that separated early in vertebrate evolution."xsd:string
http://purl.uniprot.org/citations/17804405http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m706818200"xsd:string
http://purl.uniprot.org/citations/17804405http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m706818200"xsd:string
http://purl.uniprot.org/citations/17804405http://purl.uniprot.org/core/author"Van Schaftingen E."xsd:string
http://purl.uniprot.org/citations/17804405http://purl.uniprot.org/core/author"Van Schaftingen E."xsd:string
http://purl.uniprot.org/citations/17804405http://purl.uniprot.org/core/author"Veiga-da-Cunha M."xsd:string
http://purl.uniprot.org/citations/17804405http://purl.uniprot.org/core/author"Veiga-da-Cunha M."xsd:string
http://purl.uniprot.org/citations/17804405http://purl.uniprot.org/core/author"Vertommen D."xsd:string
http://purl.uniprot.org/citations/17804405http://purl.uniprot.org/core/author"Vertommen D."xsd:string
http://purl.uniprot.org/citations/17804405http://purl.uniprot.org/core/author"Maliekal P."xsd:string
http://purl.uniprot.org/citations/17804405http://purl.uniprot.org/core/author"Maliekal P."xsd:string
http://purl.uniprot.org/citations/17804405http://purl.uniprot.org/core/author"Sokolova T."xsd:string
http://purl.uniprot.org/citations/17804405http://purl.uniprot.org/core/author"Sokolova T."xsd:string
http://purl.uniprot.org/citations/17804405http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17804405http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17804405http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17804405http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17804405http://purl.uniprot.org/core/pages"31844-31851"xsd:string
http://purl.uniprot.org/citations/17804405http://purl.uniprot.org/core/pages"31844-31851"xsd:string
http://purl.uniprot.org/citations/17804405http://purl.uniprot.org/core/title"Molecular identification of mammalian phosphopentomutase and glucose-1,6-bisphosphate synthase, two members of the alpha-D-phosphohexomutase family."xsd:string
http://purl.uniprot.org/citations/17804405http://purl.uniprot.org/core/title"Molecular identification of mammalian phosphopentomutase and glucose-1,6-bisphosphate synthase, two members of the alpha-D-phosphohexomutase family."xsd:string
http://purl.uniprot.org/citations/17804405http://purl.uniprot.org/core/volume"282"xsd:string
http://purl.uniprot.org/citations/17804405http://purl.uniprot.org/core/volume"282"xsd:string
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