EC Number   |
General Information |
Reference |
|---|
    2.7.1.47 | evolution |
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 |
-, 759480 |
| 2.7.1.47 | malfunction |
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 |
759480 |
| 2.7.1.47 | malfunction |
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 |
-, 759480 |
| 2.7.1.47 | more |
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 |
759480 |
| 2.7.1.47 | more |
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 |
-, 759480 |
| 2.7.1.47 | physiological function |
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 |
759480 |
| 2.7.1.47 | physiological function |
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 |
-, 759480 |
