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Literature summary extracted from

  • Singh, C.; Glaab, E.; Linster, C.L.
    Molecular identification of D-ribulokinase in budding yeast and mammals (2017), J. Biol. Chem., 292, 1005-1028 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

Protein Variants

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

General Stability

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

KM Value [mM]

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.47 Mg2+ required Saccharomyces cerevisiae
2.7.1.47 Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

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
-
?

Organism

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
-
-

Purification (Commentary)

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.1.47 HEK-293 cell
-
Homo sapiens
-

Substrates and Products (Substrate)

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 ?
-
-

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
2.7.1.47 FGGY
-
Homo sapiens
2.7.1.47 Ydr109c protein
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

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

pH Optimum

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

General Information

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