the FGGY protein shows a clear substrate preference for D-ribulose over a range of other sugars and sugar derivatives tested, including L-ribulose. Recombinant human FGGY protein specifically converts D-ribulose to D-ribulose 5-phosphate in the presence of ATP. No or poor activity with D-xylulose, L-xylulose, D-glucose, arabitol, erythritol, L-arabinose, D-arabinose, D-ribose, glycerol, D-ribulose 5-phosphate, gluconate, 2-deoxy-D-ribose, D-lyxose, D-ribose 5-phosphate, D-mannitol, and D-ribose 1-phosphate
the FGGY protein shows a clear substrate preference for D-ribulose over a range of other sugars and sugar derivatives tested, including L-ribulose. Recombinant human FGGY protein specifically converts D-ribulose to D-ribulose 5-phosphate in the presence of ATP. No or poor activity with D-xylulose, L-xylulose, D-glucose, arabitol, erythritol, L-arabinose, D-arabinose, D-ribose, glycerol, D-ribulose 5-phosphate, gluconate, 2-deoxy-D-ribose, D-lyxose, D-ribose 5-phosphate, D-mannitol, and D-ribose 1-phosphate
the Ydr109c protein shows a clear specificity for D-ribulose over a range of other sugars and sugar derivatives tested, including L-ribulose. Recombinant yeast Ydr109c specifically converts D-ribulose to D-ribulose 5-phosphate in the presence of ATP. No activity with L-ribulose, ribitol, D-xylulose, L-xylulose, D-glucose, arabitol, erythritol, L-arabinose, D-arabinose, D-ribose, glycerol, D-ribulose 5-phosphate, gluconate, 2-deoxy-D-ribose, D-lyxose, D-ribose 5-phosphate, D-mannitol, and D-ribose 1-phosphate
the Ydr109c protein shows a clear specificity for D-ribulose over a range of other sugars and sugar derivatives tested, including L-ribulose. Recombinant yeast Ydr109c specifically converts D-ribulose to D-ribulose 5-phosphate in the presence of ATP. No activity with L-ribulose, ribitol, D-xylulose, L-xylulose, D-glucose, arabitol, erythritol, L-arabinose, D-arabinose, D-ribose, glycerol, D-ribulose 5-phosphate, gluconate, 2-deoxy-D-ribose, D-lyxose, D-ribose 5-phosphate, D-mannitol, and D-ribose 1-phosphate
the Ydr109c protein shows a clear specificity for D-ribulose over a range of other sugars and sugar derivatives tested, including L-ribulose. Recombinant yeast Ydr109c specifically converts D-ribulose to D-ribulose 5-phosphate in the presence of ATP. No activity with L-ribulose, ribitol, D-xylulose, L-xylulose, D-glucose, arabitol, erythritol, L-arabinose, D-arabinose, D-ribose, glycerol, D-ribulose 5-phosphate, gluconate, 2-deoxy-D-ribose, D-lyxose, D-ribose 5-phosphate, D-mannitol, and D-ribose 1-phosphate
the enzyme belongs to the broadly conserved FGGY family of carbohydrate kinases. Yeast Ydr109c and human FGGY are homologues of a proteobacterial D-ribulokinase involved in ribitol metabolism
the enzyme belongs to the broadly conserved FGGY family of carbohydrate kinases. Yeast Ydr109c and human FGGY are homologues of a proteobacterial D-ribulokinase involved in ribitol metabolism
the enzyme belongs to the broadly conserved FGGY family of carbohydrate kinases. Yeast Ydr109c and human FGGY are homologues of a proteobacterial D-ribulokinase involved in ribitol metabolism
in human FGGY deletion mutant HEK293 cells, ribulose can only be detected when ribitol is added to the cultivation medium. Under this condition, FGGY silencing leads to ribulose accumulation
untargeted metabolomics analysis of an Saccharomyces cerevisiae deletion mutant of YDR109C reveals ribulose as one of the metabolites with the most significantly changed intracellular concentration as compared with a wild-type strain
untargeted metabolomics analysis of an Saccharomyces cerevisiae deletion mutant of YDR109C reveals ribulose as one of the metabolites with the most significantly changed intracellular concentration as compared with a wild-type strain
the FGGY protein might act as a metabolite repair enzyme, serving to re-phosphorylate free D-ribulose generated by promiscuous phosphatases from D-ribulose 5-phosphate
the Ydr109c protein might act as a metabolite repair enzyme, serving to re-phosphorylate free D-ribulose generated by promiscuous phosphatases from D-ribulose 5-phosphate
the Ydr109c protein might act as a metabolite repair enzyme, serving to re-phosphorylate free D-ribulose generated by promiscuous phosphatases from D-ribulose 5-phosphate
the enzyme contains a 5-residue D-ribulokinase signature motif (TCSLV). Structural homology modeling of human D-ribulokinase and definition of a D-ribulokinase signature motif, using template structures from PDB entries 3GG4 chain A and 3L0Q chain A, respectively, of Yersinia pseudotuberculosis D-ribulokinase
the enzyme contains a 5-residue D-ribulokinase signature motif (TCSLV). Structural homology modeling of human D-ribulokinase and definition of a D-ribulokinase signature motif, using template structures from PDB entries 3GG4 chain A and 3L0Q chain A, respectively, of Yersinia pseudotuberculosis D-ribulokinase
the enzyme contains a 5-residue D-ribulokinase signature motif (TCSLV). Structural homology modeling of yeast D-ribulokinase and definition of a D-ribulokinase signature motif, using template structures from PDB entries 3GG4 chain A and 3L0Q chain A, respectively, of Yersinia pseudotuberculosis D-ribulokinase
the enzyme contains a 5-residue D-ribulokinase signature motif (TCSLV). Structural homology modeling of yeast D-ribulokinase and definition of a D-ribulokinase signature motif, using template structures from PDB entries 3GG4 chain A and 3L0Q chain A, respectively, of Yersinia pseudotuberculosis D-ribulokinase
the enzyme contains a 5-residue D-ribulokinase signature motif (TCSLV). Structural homology modeling of yeast D-ribulokinase and definition of a D-ribulokinase signature motif, using template structures from PDB entries 3GG4 chain A and 3L0Q chain A, respectively, of Yersinia pseudotuberculosis D-ribulokinase
untargeted metabolomics analysis of an Saccharomyces cerevisiae deletion mutant of YDR109C reveals ribulose as one of the metabolites with the most significantly changed intracellular concentration as compared with a wild-type strain. Effect of YDR109C deletion on metabolite level other than ribulose and ribitol, overview
untargeted metabolomics analysis of an Saccharomyces cerevisiae deletion mutant of YDR109C reveals ribulose as one of the metabolites with the most significantly changed intracellular concentration as compared with a wild-type strain. Effect of YDR109C deletion on metabolite level other than ribulose and ribitol, overview
untargeted metabolomics analysis of an Saccharomyces cerevisiae deletion mutant of YDR109C reveals ribulose as one of the metabolites with the most significantly changed intracellular concentration as compared with a wild-type strain. Effect of YDR109C deletion on metabolite level other than ribulose and ribitol, overview