Reference : Molecular Identification of D-Ribulokinase in Budding Yeast and Mammals
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Life sciences : Multidisciplinary, general & others
Human health sciences : Multidisciplinary, general & others
Systems Biomedicine
Molecular Identification of D-Ribulokinase in Budding Yeast and Mammals
Singh, Charandeep [University of Luxembourg > Luxembourg Centre for Systems Biomedicine (LCSB) > >]
Glaab, Enrico mailto [University of Luxembourg > Luxembourg Centre for Systems Biomedicine (LCSB) > >]
Linster, Carole [University of Luxembourg > Luxembourg Centre for Systems Biomedicine (LCSB) > >]
Journal of Biological Chemistry
American Society for Biochemistry and Molecular Biology
Yes (verified by ORBilu)
[en] carbohydrate metabolism ; enzyme kinetics ; mass spectrometry ; metabolomics ; pentose phosphate pathway ; protein motif ; Saccharomyces cerevisiae ; structural model ; FGGY carbohydrate kinase family ; ribulose
[en] Proteomes of even well characterized organisms still contain a high percentage of proteins with unknown or uncertain molecular and/or biological function. A significant fraction of those proteins are predicted to have catalytic properties. Here we aimed at identifying the function of the Saccharomyces cerevisiae Ydr109c protein and of its human homolog FGGY, both of which belong to the broadly conserved FGGY family of carbohydrate kinases. Functionally identified members of this family phosphorylate 3- to 7-carbon sugars or sugar derivatives, but the endogenous substrate of S. cerevisiae Ydr109c and human FGGY has remained unknown. Untargeted metabolomics analysis of an S. cerevisiae deletion mutant of YDR109C revealed ribulose as one of the metabolites with the most significantly changed intracellular concentration as compared to a wild-type strain. In human HEK293 cells, ribulose could only be detected when ribitol was added to the cultivation medium and under this condition, FGGY silencing led to ribulose accumulation. Biochemical characterization of the recombinant purified Ydr109c and FGGY proteins showed a clear substrate preference of both kinases for D-ribulose over a range of other sugars and sugar derivatives tested, including L-ribulose. Detailed sequence and structural analyses of Ydr109c and FGGY as well as homologs thereof furthermore allowed the definition of a 5-residue D-ribulokinase signature motif (TCSLV). The physiological role of the herein identified eukaryotic D-ribulokinase remains unclear, but we speculate that S. cerevisiae Ydr109c and human FGGY could act as metabolite repair enzymes, serving to re-phosphorylate free D-ribulose generated by promiscuous phosphatases from D-ribulose-5-phosphate. In human cells, FGGY can additionally participate in ribitol metabolism.
Luxembourg Centre for Systems Biomedicine (LCSB): Enzymology & Metabolism (Linster Group)
Fonds National de la Recherche - FnR ; Fondation du PĂ©lican de Mie
R-STR-4006 > Enzymology & Metabolism (Linster) > 01/01/2013 - 19/01/2048 > LINSTER Carole
Researchers ; Professionals ; Students
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