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Molecular identification of mammalian phosphopentomutase and glucose-1,6-bisphosphate synthase, two members of the alpha-D-phosphohexomutase family.

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Maliekal, Pushpa Sokolova, Tatiana [UCL] Vertommen, Didier [UCL] Veiga da Cunha, Maria [UCL] Van Schaftingen, Emile [UCL]

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.

Document type Article de périodique (Journal article) – Article de recherche
Access type Accès restreint
Publication date 2007
Journal information "The Journal of biological chemistry" - Vol. 282, no. 44, p. 31844-51 (2007)
Peer reviewed yes
issn 0021-9258
Publication status Publié
Affiliation UCL - MD/BICL - Département de biochimie et de biologie cellulaire
MESH Subject Amino Acid Sequence ; Animals ; Erythrocytes - enzymology ; Evolution, Molecular ; Gene Expression Profiling ; Humans ; Male ; Mice ; Molecular Sequence Data ; Organ Specificity ; Phosphotransferases - chemistry - genetics - isolation & purification - metabolism
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Bibliographic reference Maliekal, Pushpa ; Sokolova, Tatiana ; Vertommen, Didier ; Veiga da Cunha, Maria ; Van Schaftingen, Emile. Molecular identification of mammalian phosphopentomutase and glucose-1,6-bisphosphate synthase, two members of the alpha-D-phosphohexomutase family.. In: The Journal of biological chemistry, Vol. 282, no. 44, p. 31844-51 (2007)
Permanent URL http://hdl.handle.net/2078.1/11093