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EC Tree
The taxonomic range for the selected organisms is: Hordeum vulgare The enzyme appears in selected viruses and cellular organisms
Synonyms
udp-glucose pyrophosphorylase, ugpase, udpg-pyrophosphorylase, udpgp, udp-glc pyrophosphorylase, udpglucose pyrophosphorylase, glucose-1-phosphate uridylyltransferase, udpg pyrophosphorylase, utp-glucose-1-phosphate uridylyltransferase, uridine diphosphoglucose pyrophosphorylase,
more
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UDP-glucose pyrophosphorylase
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glucose 1-phosphate uridylyltransferase
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glucose-1-phosphate uridylyltransferase
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UDP glucose pyrophosphorylase
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UDP-Glc pyrophosphorylase
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UDP-glucose pyrophosphorylase
UDPG phosphorylase
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UDPG pyrophosphorylase
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UDPglucose pyrophosphorylase
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uridine 5'-diphosphoglucose pyrophosphorylase
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uridine diphosphate-D-glucose pyrophosphorylase
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uridine diphosphoglucose pyrophosphorylase
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uridine-diphosphate glucose pyrophosphorylase
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uridylyltransferase, glucose 1-phosphate
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UDP-glucose pyrophosphorylase
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UDP-glucose pyrophosphorylase
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nucleotidyl group transfer
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UTP:alpha-D-glucose-1-phosphate uridylyltransferase
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UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
UTP + D-glucose-1-phosphate
diphosphate + UDP-glucose
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?
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
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low activity
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r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
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r
additional information
?
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the enzyme catalyses a freely reversible reaction and is specific for alpha-D-glucose 1-phosphate
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?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
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?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
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r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
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r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
key enzyme in biosynthesis of sucrose, cellulose, and other saccharides
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r
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UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
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r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
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?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
key enzyme in biosynthesis of sucrose, cellulose, and other saccharides
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r
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additional information
not inhibitory: Tween-20
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additional information
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not inhibitory: Tween-20
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dithiothreitol
increases wild-type activity by about 25%
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10
alpha-D-galactose 1-phosphate
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pH 7.5, temperature not specified in the publication
0.033
alpha-D-glucose 1-phosphate
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pH 7.5, temperature not specified in the publication
0.025
UTP
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pH 7.5, temperature not specified in the publication
additional information
additional information
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kinetics, overview
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0.027
diphosphate
Y192A mutant protein
0.03
diphosphate
Ccut-8 mutant protein
0.03
diphosphate
K183A mutant protein
0.034
diphosphate
recombinant wild-type, pH 7.6, 25°C
0.039
diphosphate
wild-type protein
0.04
diphosphate
K332A mutant protein
0.09
diphosphate
Ncut-21 mutant protein
0.24
diphosphate
K405A mutant protein
0.407
diphosphate
recombinant mutant C99S, pH 7.6, 25°C
0.9
diphosphate
Ncut-37 mutant protein
4.9
diphosphate
K260A mutant protein
6.4
diphosphate
Ccut-32 mutant protein
9.8
diphosphate
Ccut-67 mutant protein
29.4
diphosphate
Delta 1-4 mutant protein
33.3
diphosphate
Ccut-101 mutant protein
60
diphosphate
Delta 1-8 mutant protein
0.03
UDP-glucose
Ccut-8 mutant protein
0.03
UDP-glucose
K183A mutant protein
0.03
UDP-glucose
K332A mutant protein
0.031
UDP-glucose
Y192A mutant protein
0.034
UDP-glucose
wild-type protein
0.04
UDP-glucose
K405A mutant protein
0.065
UDP-glucose
recombinant wild-type, pH 7.6, 25°C
0.074
UDP-glucose
K260A mutant protein
0.101
UDP-glucose
recombinant mutant C99S, pH 7.6, 25°C
0.118
UDP-glucose
Ccut-101 mutant protein
0.31
UDP-glucose
Ccut-32 mutant protein
0.362
UDP-glucose
Ccut-67 mutant protein
0.503
UDP-glucose
Delta 1-8 mutant protein
0.555
UDP-glucose
Delta 1-4 mutant protein
1.1
UDP-glucose
Ncut-21 mutant protein
57
UDP-glucose
Ncut-37 mutant protein
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0
Delta-NB mutant protein
0.02
Ncut-37 mutant protein
0.21
Ccut-101 mutant protein
0.27
Ccut-32 mutant protein
0.42
K260A mutant protein
12.8
Ncut-21 mutant protein
1547
Ccut-8 mutant protein
2.1
Delta 1-4 mutant protein
3.1
Ccut-67 mutant protein
5.4
Delta 1-8 mutant protein
additional information
similar activities of the wild-type UGPase in Tris, Hepes or Mops buffers. Half of the activity in 100 mM sodium phosphate. Compared with the wild-type UGPase the mutants KK127-128LL, C99S and LIV135-137NIN display reduced activities in all buffers.
additional information
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similar activities of the wild-type UGPase in Tris, Hepes or Mops buffers. Half of the activity in 100 mM sodium phosphate. Compared with the wild-type UGPase the mutants KK127-128LL, C99S and LIV135-137NIN display reduced activities in all buffers.
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6.5 - 8.5
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broad optimum in both reaction directions
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4.5 - 10
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forward reaction sharp drop in activity above pH 10.0, inactive above pH 10.0 and below pH 4.0, profile overview
5.5 - 9.5
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reverse reaction, inactive above pH 10.0 and below pH 5.0, profile overview
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5.54
Ncut-21 mutant protein
5.58
Ccut-101 mutant protein
5.63
Delta 1-4 mutant protein
5.69
Ccut-67 mutant protein
5.7
Ncut-37 mutant protein
5.79
Ccut-32 mutant protein
5.8
Ccut-8 mutant protein
5.47
K183A mutant protein
5.47
K332A mutant protein
5.47
K405A mutant protein
5.55
Delta 1-8 mutant protein
5.55
Delta-NB mutant protein
5.55
Y192A mutant protein
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SwissProt
brenda
gene Ugp
SwissProt
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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developing seeds
brenda
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brenda
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brenda
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brenda
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evolution
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the plant UGPases belongs to the so called UGPase-A family
physiological function
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UDP-Glc pyrophosphorylase is an essential enzyme responsible for production of UDP-Glc, which is used in hundreds of glycosylation reactions involving addition of Glc to a variety of compounds
additional information
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structure modeling, overview. The quaternary structure of the enzyme is affected by addition of either single or both substrates in either direction of the reaction, resulting in a shift from UGPase dimers toward monomers, the active form of the enzyme. The substrate-induced changes in quaternary structure of the enzyme may have a regulatory role to assure maximal activity
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UGPA_HORVU
473
0
51644
Swiss-Prot
other Location (Reliability: 3 )
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51600
x * 51600, about, embryo, amino acid sequence determination
additional information
mixture of monomers, dimers and higher-order polymers, native PAGE and gel filtration, the monomer is the active form
additional information
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mixture of monomers, dimers and higher-order polymers, native PAGE and gel filtration, the monomer is the active form
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?
x * 51600, about, embryo, amino acid sequence determination
dimer
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inactive enzyme form
monomer
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active enzyme form
additional information
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structure modeling, overview. The quaternary structure of the enzyme is affected by addition of either single or both substrates in either direction of the reaction, resulting in a shift from UGPase dimers toward monomers, the active form of the enzyme. The substrate-induced changes in quaternary structure of the enzyme may have a regulatory role to assure maximal activity. The ratio of monomers to dimers is about 5:1 in absence of substrate
oligomer
SDS-PAGE. Incubation of wild-type UGPase with phosphate or Tris buffers promote oligomerization, whereas Mops and Hepes completely dissociate the oligomers to monomers. Similar buffer effects for mutants KK127-128LL and C99S, small buffer effects for mutant LIV135-137NIN
oligomer
x * 52000-53000, SDS-PAGE
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glycoprotein
3 putative N-glycosylation sites, possible role in intracellular targeting of the enzyme
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C99S
site-directed mutagenesis, half Vmax of wild-type, 12fold higher Km for diphosphate, altered diphosphate binding
Ccut-101
101 amino acid residues deleted (exons 16-19, and 1 amino acid residue of exon 15)
Ccut-32
32 amino acid residues deleted (exon 18 and exon 19)
Ccut-67
67 amino acid residues deleted (exons 17-19)
Ccut-8
8 amino acid residues deleted (last exon (exon 19))
Delta 1-4
deletion of 4 amino acid residues of the C-terminal domain, possibly involved in oligomerization
Delta 1-8
deletion of 8 amino acid residues of the C-terminal domain, possibly involved in oligomerization
Delta-NB
deletion mutant: amino acid residue 96-100 deleted (essential for catalysis)
K183A
possibly involved in subunit interaction
K260A
possibly involved in diphosphate binding
K332A
possibly involved in subunit interaction
K405A
possibly involved in subunit interaction
Ncut-21
21 amino acid residues deleted (exon 1)
Ncut-37
37 amino acid residues deleted (exon 1 and exon 2)
Y192A
possibly involved in UDP-glucose binding
additional information
amino acid exchanges in hydrophobic domain
additional information
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amino acid exchanges in hydrophobic domain
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immobilized metal ion affinity chromatography
native and recombinant wild-type, the latter from Escherichia coli to homogeneity
recombinant enzyme from Escherichia coli
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expression in Escherichia coli
from cDNA libraries, 11 clones, DNA and amino acid sequence determination and analysis
gene Ugp, expression in Escherichia coli
His-tag version expressed in Escherichia coli BL21 (DE3)
overexpression in Escherichia coli
expression in Escherichia coli
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Eimert, K.; Villand, P.; Kilian, A.; Kleczkowski, L.A.
Cloning and characterization of several cDNAs for UDP-glucose pyrophosphorylase from barley (Hordeum vulgare) tissues
Gene
170
227-232
1996
Hordeum vulgare (Q43772), Hordeum vulgare
brenda
Martz, F.; Wilczynska, M.; Kleczkowski, L.A.
Oligomerization status, with the monomer as active species, defines catalytic efficiency of UDP-glucose pyrophosphorylase
Biochem. J.
367
295-300
2002
Hordeum vulgare (Q43772), Hordeum vulgare
brenda
Kleczkowski, L.A.; Martz, F.; Wilczynska, M.
Factors affecting oligomerization status of UDP-glucose pyrophosphorylase
Phytochemistry
66
2815-2821
2005
Hordeum vulgare (Q43772), Hordeum vulgare
brenda
Meng, M.; Fitzek, E.; Gajowniczek, A.; Wilczynska, M.; Kleczkowski, L.A.
Domain-specific determinants of catalysis/substrate binding and the oligomerization status of barley UDP-glucose pyrophosphorylase
Biochim. Biophys. Acta
1794
1734-1742
2009
Hordeum vulgare (Q43772), Hordeum vulgare
brenda
Decker, D.; Meng, M.; Gornicka, A.; Hofer, A.; Wilczynska, M.; Kleczkowski, L.A.
Substrate kinetics and substrate effects on the quaternary structure of barley UDP-glucose pyrophosphorylase
Phytochemistry
79
39-45
2012
Hordeum vulgare
brenda
Decker, D.; Oeberg, C.; Kleczkowski, L.A.
Identification and characterization of inhibitors of UDP-glucose and UDP-sugar pyrophosphorylases for in vivo studies
Plant J.
90
1093-1107
2017
Arabidopsis thaliana (P57751), Arabidopsis thaliana (Q9M9P3), Hordeum vulgare (Q43772)
brenda