EC Number | Cloned (Comment) | Organism |
---|---|---|
2.7.1.47 | gene FGGY, sequence comparisons and phylogenetic tree, recombinant expression of N-terminally His-tagged FGGY in Escherichia coli | Homo sapiens |
2.7.1.47 | gene YDR109C, sequence comparisons and phylogenetic tree, recombinant expression of N-terminally His-tagged Ydr109c in Escherichia coli | Saccharomyces cerevisiae |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.7.1.47 | additional information | generation of human FGGY deletion mutant HEK293 cells, when ribitol is added to the cultivation medium, FGGY silencing leads to ribulose accumulation | Homo sapiens |
2.7.1.47 | additional information | 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 | Saccharomyces cerevisiae |
EC Number | General Stability | Organism |
---|---|---|
2.7.1.47 | the human recombinant His-tagged FGGY protein is, unlike its yeast homologue, very stable | Homo sapiens |
2.7.1.47 | the yeast recombinant His-tagged Ydr109c protein is, unlike its human homologue, very unstable | Saccharomyces cerevisiae |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.7.1.47 | additional information | - |
additional information | Michaelis-Menten kinetics | Saccharomyces cerevisiae | |
2.7.1.47 | 0.097 | - |
D-ribulose | pH 7.1, 30°C, recombinant enzyme | Homo sapiens | |
2.7.1.47 | 0.217 | - |
D-ribulose | pH 7.1, 30°C, recombinant enzyme | Saccharomyces cerevisiae | |
2.7.1.47 | 1.468 | - |
ribitol | pH 7.1, 30°C, recombinant enzyme | Homo sapiens |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.1.47 | Mg2+ | required | Saccharomyces cerevisiae | |
2.7.1.47 | Mg2+ | required | Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.1.47 | ATP + D-ribulose | Saccharomyces cerevisiae | - |
ADP + D-ribulose 5-phosphate | - |
? | |
2.7.1.47 | ATP + D-ribulose | Homo sapiens | - |
ADP + D-ribulose 5-phosphate | - |
? | |
2.7.1.47 | ATP + D-ribulose | Saccharomyces cerevisiae ATCC 204508 | - |
ADP + D-ribulose 5-phosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.1.47 | Homo sapiens | Q96C11 | - |
- |
2.7.1.47 | Saccharomyces cerevisiae | Q04585 | - |
- |
2.7.1.47 | Saccharomyces cerevisiae ATCC 204508 | Q04585 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.7.1.47 | recombinant N-terminally His-tagged FGGY from Escherichia coli by nickel affinity chromatography | Homo sapiens |
2.7.1.47 | recombinant N-terminally His-tagged Ydr109c from Escherichia coli by nickel affinity chromatography | Saccharomyces cerevisiae |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
2.7.1.47 | HEK-293 cell | - |
Homo sapiens | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.1.47 | ATP + D-ribulose | - |
Saccharomyces cerevisiae | ADP + D-ribulose 5-phosphate | - |
? | |
2.7.1.47 | ATP + D-ribulose | - |
Homo sapiens | ADP + D-ribulose 5-phosphate | - |
? | |
2.7.1.47 | ATP + D-ribulose | - |
Saccharomyces cerevisiae ATCC 204508 | ADP + D-ribulose 5-phosphate | - |
? | |
2.7.1.47 | ATP + L-ribulose | 8% activity compared to D-ribulose | Homo sapiens | ADP + L-ribulose 5-phosphate | - |
? | |
2.7.1.47 | ATP + ribitol | 21% activity compared to D-ribulose | Homo sapiens | ADP + ribitol phosphate | - |
? | |
2.7.1.47 | additional information | 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 | Homo sapiens | ? | - |
- |
|
2.7.1.47 | additional information | 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 | Saccharomyces cerevisiae | ? | - |
- |
|
2.7.1.47 | additional information | 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 | Saccharomyces cerevisiae ATCC 204508 | ? | - |
- |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.7.1.47 | ? | x * 63700, recombinant His-tagged FGGY, SDS-PAGE | Homo sapiens |
2.7.1.47 | ? | x * 82800, recombinant His-tagged Ydr109c, SDS-PAGE | Saccharomyces cerevisiae |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.7.1.47 | FGGY | - |
Homo sapiens |
2.7.1.47 | Ydr109c protein | - |
Saccharomyces cerevisiae |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.1.47 | 30 | - |
assay at | Saccharomyces cerevisiae |
2.7.1.47 | 30 | - |
assay at | Homo sapiens |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.7.1.47 | 7.1 | - |
assay at | Saccharomyces cerevisiae |
2.7.1.47 | 7.1 | - |
assay at | Homo sapiens |
EC Number | General Information | Comment | Organism |
---|---|---|---|
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 | Saccharomyces cerevisiae |
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 | Homo sapiens |
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 | Homo sapiens |
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 | Saccharomyces cerevisiae |
2.7.1.47 | additional information | 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 | Homo sapiens |
2.7.1.47 | additional information | 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 | Saccharomyces cerevisiae |
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 | Homo sapiens |
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 | Saccharomyces cerevisiae |