EC Number | Cloned (Comment) | Organism |
---|---|---|
2.7.7.9 | expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Saccharomyces cerevisiae |
2.7.7.9 | expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Drosophila melanogaster |
2.7.7.9 | expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Danio rerio |
2.7.7.9 | expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Caenorhabditis elegans |
2.7.7.9 | expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Homo sapiens |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.7.7.9 | purified recombinant enzyme, hanging drop vapour diffusion method, mixing of 0.002 ml of 10 mg/ml protein in 20 mM Tris/HCl, pH 8.0, and 200 mM NaCl, with 0.001 ml of reservoir solution containing 100 mM HEPES, pH 6.5, 5 mM MgSO4, 15% w/v PEG 3350 and 20% v/v glycerol, 20°C, X-ray diffraction structure determination and analysis at 3.6 A resolution, molecular replacement | Homo sapiens |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.7.7.9 | E412D | site-directed mutagenesis, the mutation does not change the oligomeric state, the mutant shows 176% catalytic activity compared to the wild-type enzyme | Homo sapiens |
2.7.7.9 | E412K | site-directed mutagenesis, the mutant has a longer side chain with a reverse in charge showed obvious inhibitory effects which results in 78% reduced activity compared to the wild-type hUGPase activity | Homo sapiens |
2.7.7.9 | E412Q | site-directed mutagenesis, the mutation changes the charge property, but not the length of side chain and shows only a marginal increase in activity of 19% when compared with the wild-type protein | Homo sapiens |
2.7.7.9 | K4110S | site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme | Homo sapiens |
2.7.7.9 | N491P/L492E | site-directed mutagenesis, mutant N491P/L492E is constructed to depolymerize hUGPase octamers, the mutation in the C-terminal left-handed beta-helix changes the oligomerization state the mutant enzyme, that becomes monomeric, it shows about the double activity of the wild-type enzyme | Homo sapiens |
2.7.7.9 | P414G/T415P | site-directed mutagenesis, the mutant shows activity similar to that of the wild-type hUGPase, the mutation does not change the oligomeric state | Homo sapiens |
2.7.7.9 | S309N/S311R | site-directed mutagenesis, mutation in sequence analogy to the Saccharomyces cerevisiae enzyme, the mutant shows 84% of wild-type activity | Homo sapiens |
2.7.7.9 | T406K/M407L | site-directed mutagenesis, the mutant shows activity similar to that of the wild-type hUGPase, the mutation does not change the oligomeric state | Homo sapiens |
2.7.7.9 | V416N | site-directed mutagenesis, the mutant shows activity similar to that of the wild-type hUGPase, the mutation does not change the oligomeric state | Homo sapiens |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.7.7.9 | 0.067 | - |
alpha-D-glucose 1-phosphate | pH 7.5, 37°C, recombinant mutant E412K | Homo sapiens | |
2.7.7.9 | 0.151 | - |
alpha-D-glucose 1-phosphate | pH 7.5, 37°C, recombinant mutant K410S | Homo sapiens | |
2.7.7.9 | 0.155 | - |
alpha-D-glucose 1-phosphate | pH 7.5, 37°C, recombinant mutant E412Q | Homo sapiens | |
2.7.7.9 | 0.183 | - |
alpha-D-glucose 1-phosphate | pH 7.5, 37°C, recombinant enzyme | Danio rerio | |
2.7.7.9 | 0.198 | - |
alpha-D-glucose 1-phosphate | pH 7.5, 37°C, recombinant mutant N491P/L492E | Homo sapiens | |
2.7.7.9 | 0.202 | - |
alpha-D-glucose 1-phosphate | pH 7.5, 37°C, recombinant mutant P414G/T415P | Homo sapiens | |
2.7.7.9 | 0.205 | - |
alpha-D-glucose 1-phosphate | pH 7.5, 37°C, recombinant mutant E412D | Homo sapiens | |
2.7.7.9 | 0.217 | - |
alpha-D-glucose 1-phosphate | pH 7.5, 37°C, recombinant mutant V416N | Homo sapiens | |
2.7.7.9 | 0.219 | - |
alpha-D-glucose 1-phosphate | pH 7.5, 37°C, recombinant mutant T406K/M407L | Homo sapiens | |
2.7.7.9 | 0.235 | - |
alpha-D-glucose 1-phosphate | pH 7.5, 37°C, recombinant mutant S309N/S311R | Homo sapiens | |
2.7.7.9 | 0.253 | - |
alpha-D-glucose 1-phosphate | pH 7.5, 37°C, recombinant enzyme | Homo sapiens | |
2.7.7.9 | 0.316 | - |
alpha-D-glucose 1-phosphate | pH 7.5, 37°C, recombinant enzyme | Drosophila melanogaster | |
2.7.7.9 | 0.715 | - |
alpha-D-glucose 1-phosphate | pH 7.5, 37°C, recombinant enzyme | Caenorhabditis elegans | |
2.7.7.9 | 0.83 | - |
alpha-D-glucose 1-phosphate | pH 7.5, 37°C, recombinant enzyme | Saccharomyces cerevisiae |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.7.9 | Mg2+ | required | Homo sapiens | |
2.7.7.9 | Mg2+ | required | Saccharomyces cerevisiae |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.7.7.9 | 55000 | - |
8 * 55000, SDS-PAGE, human UGPase forms octamers through end-to-end and side-by-side interactions, structure, overview | Homo sapiens |
2.7.7.9 | 55000 | - |
8 * 55000, SDS-PAGE, the C-terminal left-handed beta-helices are important for the formation of the yUGPase octamer | Saccharomyces cerevisiae |
2.7.7.9 | 79000 | - |
1 * 79000, mutant enzyme N491P/L492E, SDS-PAGE, depolymerization of hUGPase, like in mutant N491P/L492E, results in monomers and higher enzymatic activity | Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.9 | UTP + alpha-D-glucose 1-phosphate | Homo sapiens | - |
diphosphate + UDP-glucose | - |
r | |
2.7.7.9 | UTP + alpha-D-glucose 1-phosphate | Saccharomyces cerevisiae | - |
diphosphate + UDP-glucose | - |
r | |
2.7.7.9 | UTP + alpha-D-glucose 1-phosphate | Drosophila melanogaster | - |
diphosphate + UDP-glucose | - |
r | |
2.7.7.9 | UTP + alpha-D-glucose 1-phosphate | Danio rerio | - |
diphosphate + UDP-glucose | - |
r | |
2.7.7.9 | UTP + alpha-D-glucose 1-phosphate | Caenorhabditis elegans | - |
diphosphate + UDP-glucose | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.7.9 | Caenorhabditis elegans | Q9XUS5 | - |
- |
2.7.7.9 | Danio rerio | B8JMZ1 | - |
- |
2.7.7.9 | Drosophila melanogaster | A5XCL5 | - |
- |
2.7.7.9 | Homo sapiens | Q16851 | isoform II | - |
2.7.7.9 | Saccharomyces cerevisiae | C7GP37 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.7.7.9 | recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration | Saccharomyces cerevisiae |
2.7.7.9 | recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration | Drosophila melanogaster |
2.7.7.9 | recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration | Danio rerio |
2.7.7.9 | recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration | Caenorhabditis elegans |
2.7.7.9 | recombinnat His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration | Homo sapiens |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.9 | UTP + alpha-D-glucose 1-phosphate | - |
Homo sapiens | diphosphate + UDP-glucose | - |
r | |
2.7.7.9 | UTP + alpha-D-glucose 1-phosphate | - |
Saccharomyces cerevisiae | diphosphate + UDP-glucose | - |
r | |
2.7.7.9 | UTP + alpha-D-glucose 1-phosphate | - |
Drosophila melanogaster | diphosphate + UDP-glucose | - |
r | |
2.7.7.9 | UTP + alpha-D-glucose 1-phosphate | - |
Danio rerio | diphosphate + UDP-glucose | - |
r | |
2.7.7.9 | UTP + alpha-D-glucose 1-phosphate | - |
Caenorhabditis elegans | diphosphate + UDP-glucose | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.7.7.9 | homooctamer | 8 * 55000, SDS-PAGE, human UGPase forms octamers through end-to-end and side-by-side interactions, structure, overview | Homo sapiens |
2.7.7.9 | homooctamer | 8 * 55000, SDS-PAGE, the C-terminal left-handed beta-helices are important for the formation of the yUGPase octamer | Saccharomyces cerevisiae |
2.7.7.9 | monomer | 1 * 79000, mutant enzyme N491P/L492E, SDS-PAGE, depolymerization of hUGPase, like in mutant N491P/L492E, results in monomers and higher enzymatic activity | Homo sapiens |
2.7.7.9 | More | structure comparison of human and yeast enzyme, overview | Homo sapiens |
2.7.7.9 | More | structure comparison of human and yeast enzyme, overview | Saccharomyces cerevisiae |
2.7.7.9 | octamer | - |
Drosophila melanogaster |
2.7.7.9 | octamer | - |
Danio rerio |
2.7.7.9 | octamer | - |
Caenorhabditis elegans |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.7.7.9 | UDP-glucose pyrophosphorylase | - |
Homo sapiens |
2.7.7.9 | UDP-glucose pyrophosphorylase | - |
Saccharomyces cerevisiae |
2.7.7.9 | UDP-glucose pyrophosphorylase | - |
Drosophila melanogaster |
2.7.7.9 | UDP-glucose pyrophosphorylase | - |
Danio rerio |
2.7.7.9 | UDP-glucose pyrophosphorylase | - |
Caenorhabditis elegans |
2.7.7.9 | UGPase | - |
Homo sapiens |
2.7.7.9 | UGPase | - |
Saccharomyces cerevisiae |
2.7.7.9 | UGPase | - |
Drosophila melanogaster |
2.7.7.9 | UGPase | - |
Danio rerio |
2.7.7.9 | UGPase | - |
Caenorhabditis elegans |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.7.9 | 37 | - |
assay at | Homo sapiens |
2.7.7.9 | 37 | - |
assay at | Saccharomyces cerevisiae |
2.7.7.9 | 37 | - |
assay at | Drosophila melanogaster |
2.7.7.9 | 37 | - |
assay at | Danio rerio |
2.7.7.9 | 37 | - |
assay at | Caenorhabditis elegans |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.7.7.9 | 7.5 | - |
assay at | Homo sapiens |
2.7.7.9 | 7.5 | - |
assay at | Saccharomyces cerevisiae |
2.7.7.9 | 7.5 | - |
assay at | Drosophila melanogaster |
2.7.7.9 | 7.5 | - |
assay at | Danio rerio |
2.7.7.9 | 7.5 | - |
assay at | Caenorhabditis elegans |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.7.7.9 | additional information | structure comparison of human and yeast enzyme, overview | Saccharomyces cerevisiae |
2.7.7.9 | additional information | structure comparison of human and yeast enzyme, overview. Depolymerization of hUGPase, like in mutant N491P/L492E, results in monomers and higher enzymatic activity | Homo sapiens |
2.7.7.9 | physiological function | the enzyme is essential for survival | Saccharomyces cerevisiae |