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Literature summary extracted from

  • Yu, Q.; Zheng, X.
    The crystal structure of human UDP-glucose pyrophosphorylase reveals a latch effect that influences enzymatic activity (2012), Biochem. J., 442, 283-291.
    View publication on PubMed

Cloned(Commentary)

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

Crystallization (Commentary)

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

Protein Variants

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

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

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
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

General Information

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