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Enzyme Nomenclature
Information on EC 2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase
for references in articles please use BRENDA:EC2.7.7.9
Word Map on EC 2.7.7.9
- 2.7.7.9
- phosphoglucomutase
- glycogen
- udp-galactose
- adp-glucose
- dictyostelium
-
exopolysaccharide
- udp-n-acetylglucosamine
- galactose-1-phosphate
- udp-sugars
-
udp-glucuronic
- galactokinase
- uridyltransferase
-
leloir
- xylinum
-
pyrophosphorolysis
-
sucrose-phosphate
- fructokinase
- gellan
-
aureobasidium
-
glc-1-p
- agriculture
- medicine
- synthesis
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
2.7.7.9
-
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RECOMMENDED NAME
GeneOntology No.
UTP-glucose-1-phosphate uridylyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
sequential ordered bi bi reaction mechanism
-
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
sequential ordered bi bi reaction mechanism
-
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
mechanism
-
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
mechanism
-
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
mechanism
-
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
mechanism
-
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
mechanism
-
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
mechanism
-
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
Trp333 and Arg391 are essential for activity, while His266, Arg389, Arg422, Arg 445, and Trp218 are not
-
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
sequential ordered bi bi reaction mechanism
-
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
ordered bi-bi mechanism. The molecular geometry at position 4 of glucose is responsible for substrate specificity. The gamma-phosphate group of UTP is essential for binding and for induction of the open conformation, which then allows entry of glucose 1-phosphate
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
ordered sequential Bi Bi mechanism, overview. Pyrimidine bases may approach the base binding site, but they cannot form the tight interactions observed in the HpUGPase/UDP-Glc complex. Thymine binding would be hindered by its extra methyl group, and cytosine could not make specific hydrogen bonds
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
UTP:alpha-D-glucose-1-phosphate uridylyltransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9026-22-6
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
in addition to UGPase, presence of dual substrate UDP-hexose pyrophosphorylase
SwissProt
recombinant protein. Enzyme is part of the validamycin A biosynthetic pathway
-
-
recombinant protein. Enzyme is part of the validamycin A biosynthetic pathway
-
-
ecotype Columbia for wild-type, ecotype Bensheim for transgenic plants; gene Ugp, inducible by exogenous sucrose, light and cold stress
-
-
several mutant strains, some derived from wild-type parent strain AB1133
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
a feature that discriminates UGPs of different species is the quaternary organization. While UGPs in protists are monomers, di- and tetrameric forms exist in bacteria, and the enzyme from yeast and human are octameric UGPs
malfunction
-
lack of sulfoquinovosyldiacylglycerol in the Arabidopsis ugp3 knockout mutant. The mutant does not show significant differences in glycosides and saccharides between wild type and ugp3 mutants
malfunction
-
lack of sulfoquinovosyldiacylglycerol in the Arabidopsis ugp3 knockout mutant. The mutant does not show significant differences in glycosides and saccharides between wild type and ugp3 mutants
metabolism
-
UDPG-pyrophosphorylase is the key enzyme involved in pullulan biosynthesis and pullulan production by Aureobasidium pullulans
metabolism
the enzyme catalyzes the last and reversible step of the de novo UDP-Glc biosynthetic pathway
metabolism
-
UGP2 is unable to replace UGP1 in the UGP1 knockout lines, even though it bears similar metabolic functions to UGP. The majority of proteins that are responsive to FB1 treatment are located in the chloroplast and have functions associated with photosynthesis
metabolism
-
the enzyme is important in sulfoquinovosyldiacylglycerol, SQDG, biosynthesis in chloroplasts together with UDP-sulfoquinovose synthase, SQD1 EC 3.13.1.1, and SQDG synthase, SQD2, mechanism for SQDG biosynthesis, overview. Sulfoquinovosyldiacylglycerol is the only sulfur-containing anionic glycerolipid, a relatively minor relatively minor, and is the least prevalent component of photosynthetic membrane lipids. The function of SQDG under phosphate-limited growth conditions is highly correlated with the regulation of other plant glycerolipid biosyntheses. UGP3 is not involved in the biosynthesis of secondary metabolites and cellulose, but rather is likely to be specifically involved in SQDG synthesis
metabolism
-
the enzyme is important in sulfoquinovosyldiacylglycerol, SQDG, biosynthesis in chloroplasts together with UDP-sulfoquinovose synthase, SQD1 EC 3.13.1.1, and SQDG synthase, SQD2, mechanism for SQDG biosynthesis, overview. Sulfoquinovosyldiacylglycerol is the only sulfur-containing anionic glycerolipid, a relatively minor relatively minor, and is the least prevalent component of photosynthetic membrane lipids. The function of SQDG under phosphate-limited growth conditions is highly correlated with the regulation of other plant glycerolipid biosyntheses. UGP3 is not involved in the biosynthesis of secondary metabolites and cellulose, but rather is likely to be specifically involved in SQDG synthesis
metabolism
-
UGP2 is unable to replace UGP1 in the UGP1 knockout lines, even though it bears similar metabolic functions to UGP. The majority of proteins that are responsive to FB1 treatment are located in the chloroplast and have functions associated with photosynthesis
-
metabolism
-
UDPG-pyrophosphorylase is the key enzyme involved in pullulan biosynthesis and pullulan production by Aureobasidium pullulans
-
metabolism
-
the enzyme catalyzes the last and reversible step of the de novo UDP-Glc biosynthetic pathway
-
physiological function
UDP-glucose is the onyl precuror for UDP-galactose synthesis, which is one of the sugar nucleotides essentially required for the parasite's survival and infectivity. UDP-glucose is also the glucosyl donor for the unfolded glycoprotein glucosyltransferase involved in glycoprotein quality control in the endoplasmic reticulum and is the presumed donor for the synthesis of base J, i.e. beta-D-glucosyl-hydroxymethyluracil, a rare deoxynucleotide found in telomereproximal DNA in the bloodstream form of the parasite
physiological function
-
the enzyme is a critical factor that regulates FB1-induced programmed cell death, an active form of cell suicide that is tightly regulated at the genetic level, only being activated when required, mechanism, overview
physiological function
the enzyme plays an important role in Streptococcus zooepidemicus cell envelope hyaluronic acid biosynthesis and it is also recognized as a virulence determinant in several bacterial species
physiological function
OsUgp2 plays an important role in pollen starch accumulation, complicated transcriptional regulation of OsUgp2. The spatio-temporal expression of the gene is mostly codetermined by the types, numbers and positions of cisregulatory elements within the promoter region
physiological function
UGPase is crucial in carbohydrate metabolism since UDP-Glc is used for the biosynthesis of glycogen and many other carbohydrate derivatives such as glycolipids, glycoproteins and proteoglycans
physiological function
-
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
physiological function
-
UGP3 is a plastid UDP-glucose pyrophosphorylase that supplies UDP-glucose to UDP-sulfoquinovose synthase, SQD1, in plastids
physiological function
-
UGP3 is a plastid UDP-glucose pyrophosphorylase that supplies UDP-glucose to UDP-sulfoquinovose synthase, SQD1, in plastids
physiological function
-
a knockdown mutant of Ugp1 exhibits an impaired mobilization of glycogen and trehalose as well as a reduction in oxidative stress resistance and long-term cell survival during stationary phase. The modulation of Ugp1 level readjusts glycogen and trehalose accumulation in the protein kinase A-related gene mutants. The protein kinase A-dependent phenotypes of oxidative stress resistance and long-term cell survival are also alleviated via adjustment of Ugp1 level
physiological function
UGP gene silencing by RNAi results in changes in the levels of the intermediate metabolites D-glucose 1-phosphate and UDP-glucose. The compounds and structure of the cell wall in the silenced strains are also altered compared with those in the wild-type strains. The number of hyphal branches is also changed in the silenced strains. In an UGP over-expressing strain, the number of hyphal branches is influenced by UGP. Hyphal branching is regulated by a change in the cytosolic Ca2+ concentration, which is affected by the level of the intermediate metabolite Glc-1-P
physiological function
overexpression of UGPase enhances vegetative growth in transgenic Arabidopsis thaliana and increases the contents of soluble sugars and cellulose, and thickens parenchyma cell walls
physiological function
-
the enzyme is a critical factor that regulates FB1-induced programmed cell death, an active form of cell suicide that is tightly regulated at the genetic level, only being activated when required, mechanism, overview
-
physiological function
-
UDP-glucose is the onyl precuror for UDP-galactose synthesis, which is one of the sugar nucleotides essentially required for the parasite's survival and infectivity. UDP-glucose is also the glucosyl donor for the unfolded glycoprotein glucosyltransferase involved in glycoprotein quality control in the endoplasmic reticulum and is the presumed donor for the synthesis of base J, i.e. beta-D-glucosyl-hydroxymethyluracil, a rare deoxynucleotide found in telomereproximal DNA in the bloodstream form of the parasite
-
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
additional information
structure comparison of human and yeast enzyme, overview
additional information
UDP-Glc is bound in a deep cleft located at the center of the catalytic domain that consists of highly conserved residues
additional information
-
UDP-Glc is bound in a deep cleft located at the center of the catalytic domain that consists of highly conserved residues
additional information
-
hUGPs are active in the octameric state and do not dissociate during the enzymatic cycle, structure-function relationships analysis, overview
additional information
structure-function analysis, homology modeling
additional information
-
structural basis for the reaction mechanism of UDP-glucose pyrophosphorylase, overview. The active sites are located in a deep pocket of each subunit. The tetramerization of HpUGPase does not seem to be related to allosterism
additional information
structural basis for the reaction mechanism of UDP-glucose pyrophosphorylase, overview. The active sites are located in a deep pocket of each subunit. The tetramerization of HpUGPase does not seem to be related to allosterism
additional information
-
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
additional information
-
UDP-Glc is bound in a deep cleft located at the center of the catalytic domain that consists of highly conserved residues
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
13.7% of the activity with UTP
-
r
farnesyl triphosphate + UDP-glucose
farnesyl-tetraphosphouridine + alpha-D-glucose + diphosphate
-
-
-
-
?
geranyl triphosphate + UDP-glucose
geranyl-tetraphosphouridine + alpha-D-glucose + diphosphate
-
-
-
-
?
isopentenyl triphosphate + UDP-glucose
isopentenyl-tetraphosphouridine + alpha-D-glucose + diphosphate
-
-
-
-
?
methylenebisphosphonate + UDP-glucose
uridine 5'-(beta,gamma-methylenetriphosphate) + alpha-D-glucose + diphosphate
-
-
-
-
?
monothiodiphosphate + UDP-glucose
UTPbeta,gammaS + alpha-D-glucose 1-phosphate
-
poor substrate, 4.8% of Vmax with diphosphate
UTPbeta,gammaS is chemically unstable and undergoes hydrolysis to UDPbetaS and phosphate, which renders the otherwise reversible reaction irreversible, t1/2 at 25°C: 0.5 min
ir
UDP-glucose + adenosine 5'-tetraphosphate
D-glucose-1-phosphate + adenosyl-5'-pentaphospho-5'-uridine
-
-
-
-
?
UDP-glucose + ATP
D-glucose-1-phosphate + adenosyl-5'-tetraphospho-5'-uridine
-
-
-
-
?
UDP-glucose + CTP
D-glucose-1-phosphate + cytidinyl-5'-tetraphospho-5'-uridine
-
-
-
-
?
UDP-glucose + GTP
D-glucose-1-phosphate + guanosyl-5'-tetraphospho-5'-uridine
-
-
-
-
?
UDP-glucose + guanosine 5'-tetraphosphate
D-glucose-1-phosphate + guanosyl-5'-pentaphospho-5'-uridine
-
-
-
-
?
UDP-glucose + tetrapolyphosphate
uridine-5'-pentaphosphate + D-glucose-1-phosphate
-
-
-
-
?
UDP-glucose + tripolyphosphate
uridine-5'-tetraphosphate + D-glucose-1-phosphate
-
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
UTP + alpha-D-glucose 1-phosphate
enzyme is highly specific for both UTP and glucose 1-phosphate
-
-
r
diphosphate + CDP-glucose
CTP + alpha-D-glucose 1-phosphate
-
no activity
-
-
-
diphosphate + CDP-glucose
CTP + alpha-D-glucose 1-phosphate
-
calf and human liver, poor substrate
-
r
diphosphate + CDP-glucose
CTP + alpha-D-glucose 1-phosphate
-
calf and human liver, poor substrate
-
r
diphosphate + CDP-glucose
CTP + alpha-D-glucose 1-phosphate
-
very low activity, wild-type and mutant W218
-
r
diphosphate + CDP-glucose
CTP + alpha-D-glucose 1-phosphate
-
18.5% of the activity with UTP
-
r
diphosphate + CDP-glucose
CTP + alpha-D-glucose 1-phosphate
-
no activity
-
-
-
diphosphate + GDP-glucose
GTP + alpha-D-glucose 1-phosphate
-
no activity
-
-
-
diphosphate + GDP-glucose
GTP + alpha-D-glucose 1-phosphate
-
calf and human liver, poor substrate
-
-
r
diphosphate + GDP-glucose
GTP + alpha-D-glucose 1-phosphate
-
calf and human liver, poor substrate
-
-
r
diphosphate + GDP-glucose
GTP + alpha-D-glucose 1-phosphate
-
14.3% of the activity with UTP
-
r
diphosphate + GDP-glucose
GTP + alpha-D-glucose 1-phosphate
-
no activity
-
-
-
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
-
no activity
-
-
-
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
-
poor substrate
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
-
poor substrate
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
-
calf and human liver
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
-
poor substrate
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
-
poor substrate
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
-
poor substrate
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
-
calf and human liver
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
-
very low activity, wild-type and mutant W218
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
-
poor substrate
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
-
poor substrate
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
-
poor substrate
-
r
diphosphate + UDP-glucose
UTP + alpha-D-glucose 1-phosphate
-
-
-
?
diphosphate + UDP-glucose
UTP + alpha-D-glucose 1-phosphate
-
-
-
?
diphosphate + UDP-mannose
UTP + D-mannose 1-phosphate
-
calf and human liver, poor substrate
-
-
r
diphosphate + UDP-mannose
UTP + D-mannose 1-phosphate
-
calf and human liver, poor substrate
-
-
r
diphosphate + UDP-xylose
UTP + D-xylose 1-phosphate
-
reaction at 10% the rate of UDP-glucose or UDP-galactose pyrophosphorolysis
-
-
r
diphosphate + UDP-xylose
UTP + D-xylose 1-phosphate
-
poor substrate
-
-
r
diphosphate + UDP-xylose
UTP + D-xylose 1-phosphate
-
calf and human liver
-
-
r
diphosphate + UDP-xylose
UTP + D-xylose 1-phosphate
-
poor substrate
-
-
r
diphosphate + UDP-xylose
UTP + D-xylose 1-phosphate
-
calf and human liver
-
-
r
TTP + alpha-D-glucose 1-phosphate
diphosphate + alpha-TDP-glucose
-
-
-
?
TTP + alpha-D-glucose 1-phosphate
diphosphate + alpha-TDP-glucose
-
-
-
?
TTP + alpha-D-glucose 1-phosphate
TDP-glucose + diphosphate
Q4UVD0
-
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + alpha-UDP-galactose
-
-
-
?
UTP + alpha-D-galactose 1-phosphate
diphosphate + alpha-UDP-galactose
-
-
-
?
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-alpha-D-galactose
-
-
-
?
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-alpha-D-galactose
-
-
-
?
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
-
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
-
at the same rate as UDP-glucose
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
-
about 15% of the activity with UDP-glucose
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
-
reverse reaction: calf and human liver
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
-
no activity
-
-
-
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
-
reaction at 5% the rate of UDP-glucose synthesis
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
-
reverse reaction: calf and human liver
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
-
1-12% of the activity with UDP-glucose
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
-
low activity
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
-
no activity
-
-
-
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
-
-
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
-
equilibrium dialysis: 8 mol UDP-galactose bound per mol enzyme
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
-
3.5% of the activity with UDP-glucose
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
-
-
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + alpha-UDP-glucose
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + alpha-UDP-glucose
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + alpha-UDP-glucose
-
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + alpha-UDP-glucose
-
enzyme is highly specific for UTP and glucose 1-phosphate
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
highly specific for UTP
specific for UDP-glucose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
reverse reaction: highly specific for UDP-glucose
specific for UDP-glucose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
enzyme is induced during amoeba encystment
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
highly specific for UTP
specific for UDP-glucose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
reverse reaction: highly specific for UDP-glucose
specific for UDP-glucose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
enzyme is induced during amoeba encystment
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
Acetabularia sp.
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
reaction at the same rate as UDP-galactose
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
specific for alpha-D-glucose 1-phosphate
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
central reaction in galactose and trehalose metabolism
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
the soluble enzyme shows an apparent higher affinity for and a 2fold higher activity with alpha-D-glucose 1-phosphate than UTP
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
reaction critical to mono- and polysaccharide biosynthesis
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
specific for alpha-D-glucose 1-phosphate
specific for UDP-glucose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
highly specific for UTP
specific for UDP-glucose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
key enzyme in biosynthesis of sucrose, cellulose, and other saccharides
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
cumulative feedback regulation in vivo, modulates the flow of carbon into pathways leading to cell wall polysaccharide synthesis
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
specific for alpha-D-glucose 1-phosphate
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
equilibrium dialysis: 8 mol UDP-glucose bound per mol enzyme
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
reverse reaction: highly specific for UDP-glucose
specific for UDP-glucose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
highly specific for UTP
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
enzyme is essential for cell viability
-
-
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
Saccharomyces fragilis
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
highly specific for UTP
specific for UDP-glucose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
reverse reaction: highly specific for UDP-glucose
specific for UDP-glucose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
enzyme is specific for UTP
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
enzyme is specific for UTP
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
involved in exopolysaccharide biosynthesis
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
involved in exopolysaccharide biosynthesis
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
the multifunctional enzyme also shows activity with UTP + alpha-D-glucose 1-phosphate (EC 2.7.7.24, glucose-1-phosphate thymidylyltransferase), UTP + N-acetylglucosamine 1-phosphate (EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase), dTTP + N-acetylglucosamine 1-phosphate (N-acetylglucosamine 1-phosphate thymidylyltransferase), dCTP + alpha-D-glucose 1-phosphate (glucose-1-phosphate cytidylyltransferase), dGTP + alpha-D-glucose 1-phosphate (glucose-1-phosphate guanylyltransferase), dATP + alpha-D-glucose 1-phosphate (glucose-1-phosphate adenylyltransferase). No activity with: alpha-D-glucose 1-phosphate + dATP, alpha-D-glucose 1-phosphate + dCTP, alpha-D-glucose 1-phosphate + dGTP, UTP + alpha-D-mannose1-phosphate, UTP + alpha-D-galactose 1-phosphate, UTP + alpha-D-glucosamine 1-phosphate
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
the multifunctional enzyme also shows activity with UTP + alpha-D-glucose 1-phosphate (EC 2.7.7.24, glucose-1-phosphate thymidylyltransferase), UTP + N-acetylglucosamine 1-phosphate (EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase), dTTP + N-acetylglucosamine 1-phosphate (N-acetylglucosamine 1-phosphate thymidylyltransferase), dCTP + alpha-D-glucose 1-phosphate (glucose-1-phosphate cytidylyltransferase), dGTP + alpha-D-glucose 1-phosphate (glucose-1-phosphate guanylyltransferase), dATP + alpha-D-glucose 1-phosphate (glucose-1-phosphate adenylyltransferase). No activity with: alpha-D-glucose 1-phosphate + dATP, alpha-D-glucose 1-phosphate + dCTP, alpha-D-glucose 1-phosphate + dGTP, UTP + alpha-D-mannose1-phosphate, UTP + alpha-D-galactose 1-phosphate, UTP + alpha-D-glucosamine 1-phosphate
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
UDP-glucose + diphosphate
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
UDP-glucose + diphosphate
-
14.2% activity with galactose-1-phosphate
-
-
?
UTP + alpha-D-glucose 1-phosphate
UDP-glucose + diphosphate
Q4UVD0
in the presence of a divalent metal cation (mainly Mg2+)
-
-
r
UTP + alpha-D-glucose 1-phosphate
UDP-glucose + diphosphate
in the presence of a divalent metal cation (mainly Mg2+)
-
-
r
additional information
?
-
-
no activity with ATP, CTP, and GTP
-
-
-
additional information
?
-
-
no activity with ADP-glucose
-
-
-
additional information
?
-
-
no activity with ATP, CTP, and GTP
-
-
-
additional information
?
-
-
UDP-glucose and UDP-galactose pyrophosphorolysis activity in Bifidobacterium bifidum are catalyzed by a single enzyme protein
-
-
-
additional information
?
-
-
UDP-glucose and UDP-galactose pyrophosphorolysis activity in Bifidobacterium bifidum are catalyzed by a single enzyme protein
-
-
-
additional information
?
-
the activity of UgpA toward glucose 1-phosphate is about 33fold higher than that toward galactose 1-phosphate
-
-
-
additional information
?
-
the activity of UgpA toward glucose 1-phosphate is about 33fold higher than that toward galactose 1-phosphate
-
-
-
additional information
?
-
no substrate: alpha-D-glalctose 1-phosphate
-
-
-
additional information
?
-
-
involved in synthesis of hemagglutinin, sulfated proteoglycans, and glycogen in cartilage
-
-
-
additional information
?
-
no substrates: ATP, GTP, nor CTP
-
-
-
additional information
?
-
no substrates: ATP, GTP, nor CTP
-
-
-
additional information
?
-
-
the enzyme catalyses a freely reversible reaction and is specific for alpha-D-glucose 1-phosphate
-
-
-
additional information
?
-
-
molecular geometry at position 4 of glucose is responsible for substrate specificity. The gamma-phosphate group of UTP is essential for binding and for induction of the open conformation, which then allows entry of glucose 1-phosphate
-
-
-
additional information
?
-
molecular geometry at position 4 of glucose is responsible for substrate specificity. The gamma-phosphate group of UTP is essential for binding and for induction of the open conformation, which then allows entry of glucose 1-phosphate
-
-
-
additional information
?
-
isoform Ugp1 is required for callose deposition during pollen mother cell meiosis and bridges the apoplastic unloading pathway and pollen development
-
-
-
additional information
?
-
-
no utilization of the nucleotide diphosphate sugars UDP-Gal, UDP-GlnA, UDP-Man, UDP-Xyl, ADP-Glc, CDP-Glc and TDP-Glc
-
-
-
additional information
?
-
-
UDP-galactose is not a UMP-donor and ADP not a UMP-acceptor
-
-
-
additional information
?
-
-
the bisphosphonates alendronate, pamidronate, clodronate and etidronate are not acceptors of UMP. But UDP-glucose serves as uridylyl donor to triphosphate derivatives of the mevalonate pathway, farnesyl triphosphate, geranyl triphosphate, and isopentenyl triphosphate, with formation of farnesyl-tetraphosphouridine, geranyl-tetraphosphouridine, and isopentenyl-tetraphosphouridine, overview. No activity with farnesyl-, geranyl-, or isopentenyl-diphosphates or with dimethylallyl pyrophosphate
-
-
-
additional information
?
-
no substrates: dTTP, CTP, ATP, and GTP, Glc-1P, GlcNAc-1P, Gal-1P, and Man-1P
-
-
-
additional information
?
-
-
no substrates: dTTP, CTP, ATP, and GTP, Glc-1P, GlcNAc-1P, Gal-1P, and Man-1P
-
-
-
additional information
?
-
the enzyme is specific for alpha-D-glucose 1-phosphate, no activity with N-acetylgalactosamine 1-phosphate, N-acetylglucosamine 1-phosphate, or galactosamine 1-phosphate
-
-
-
additional information
?
-
-
the enzyme is specific for alpha-D-glucose 1-phosphate, no activity with N-acetylgalactosamine 1-phosphate, N-acetylglucosamine 1-phosphate, or galactosamine 1-phosphate
-
-
-
additional information
?
-
the enzyme is specific for alpha-D-glucose 1-phosphate, no activity with N-acetylgalactosamine 1-phosphate, N-acetylglucosamine 1-phosphate, or galactosamine 1-phosphate
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UTP + alpha-D-glucose 1-phosphate
diphosphate + alpha-UDP-glucose
-
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
enzyme is induced during amoeba encystment
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
enzyme is induced during amoeba encystment
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
Acetabularia sp.
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
Q9XUS5
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
A5XCL5
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
central reaction in galactose and trehalose metabolism
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
reaction critical to mono- and polysaccharide biosynthesis
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
O25363
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
Q43772
key enzyme in biosynthesis of sucrose, cellulose, and other saccharides
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
cumulative feedback regulation in vivo, modulates the flow of carbon into pathways leading to cell wall polysaccharide synthesis
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
C7GP37
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
enzyme is essential for cell viability
-
-
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
Q8GQP8
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
involved in exopolysaccharide biosynthesis
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
involved in exopolysaccharide biosynthesis
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
D3HTY9
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
D3HTY9
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
additional information
?
-
-
involved in synthesis of hemagglutinin, sulfated proteoglycans, and glycogen in cartilage
-
-
-
additional information
?
-
A3QQQ3
isoform Ugp1 is required for callose deposition during pollen mother cell meiosis and bridges the apoplastic unloading pathway and pollen development
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Magnesium
Q6M6R3
crystallization data, two magnesium ions coordinate to UDP-glucose. Magnesium is involved in catalytic mechanism
Mg2+
Mn2+
Ni2+
additional information
Co2+
-
activation; no effect on liver enzyme form I, 2fold activation of enzyme form from sublingual gland, inhibition of enzyme form from submandibular gland
Co2+
-
about 25% as effective as Mg2+
Mg2+
-
Mg-diphosphate is the actual substrate; MgUTP is the actual substrate; requirement
Mg2+
the Mg2+ ion coordinated by Asp130, two oxygen atoms of phosphoryl groups, and three water molecules with octahedral geometry. The Mg2+ ion plays a key role in the enzymatic activity of UGPase by enhancing the binding of UGPase to UTP or UDP-glucose
Mg2+
-
Mg-diphosphate is the actual substrate; MgUTP is the actual substrate; requirement
Mg2+
-
increasing MgSO4 concentrations shift the apparent equilibrium toward UDP-glucose synthesis; Mg-diphosphate is the actual substrate; requirement
Mn2+
-
about 25% as effective as Mg2+; activation
Mn2+
-
about 25% as effective as Mg2+; activation; UDP-glucose synthesis: Mn2+ in excess of diphosphate-concentration inhibits
Ni2+
-
about 25% as effective as Mg2+
additional information
the enzyme is divalent cation-dependent, no activation by Zn2+ and Cu2+
additional information
-
the enzyme is divalent cation-dependent, no activation by Zn2+ and Cu2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
H2O2
complete loss of activity after 30 min, inactivation is reverted by reduction by cysteine and thioredoxin
iodoacetamide
-
wild-type: loss of 56% activity after 30 min at 0.1 mM, mutant C123S is not affected
NAD+
presence of either NAD or NADP results in a decrease of activity to about 80% or 50%, respectively
NADP+
presence of either NAD or NADP results in a decrease of activity to about 80% or 50%, respectively
sodium nitroprusside
complete loss of activity after 30 min, inactivation is reverted by reduction by cysteine and thioredoxin
Co2+
-
no effect on liver enzyme form I, 2fold activation of enzyme form from sublingual gland, inhibition of enzyme form from submandibular gland
Co2+
-
in excess of diphosphate-concentration, activates at lower concentrations
diphosphate
-
with 0.25 mM 57% activity, with 1 mM 11% activity, with 10 mM 1.5% activity
diphosphate
-
possible alternate regulatory mechanism; product inhibition
Mn2+
-
in excess of diphosphate-concentration, activates at lower concentrations
UDP-glucose
-
UDP-galactose pyrophosphorolysis or UDP-glucose synthesis
UDP-glucose
-
competitive to UTP, noncompetitive to glucose 1-phosphate
additional information
-
no effect of PCMB, iodoacetate, 2-mercaptoethanol or DTT
-
additional information
-
inhibition kinetics for UDP-sugars; little or no inhibition by alpha-D-mannose 1-phosphate, alpha-D-xylose 1-phosphate or alpha-D-glucuronic acid 1-phosphate
-
additional information
not inhibitory: 1 mM 2-oxoglutaric acid, 3-phosphoglyceric acid, and 5-aminolevulinic acid
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Co2+
-
no effect on liver enzyme form I, 2fold activation of enzyme form from sublingual gland, inhibition of enzyme form from submandibular gland
additional information
-
enzyme expression is inducible by exogenous sucrose, light and cold stress
-
additional information
-
no effect of PCMB, iodoacetate, 2-mercaptoethanol or DTT
-
additional information
-
rat mammary gland enzyme seems to undergo structural changes that lead to a more active form
-
additional information
-
no activation by 3-phosphoglycerate; no activation by fructose 2,6-bisphosphate, UDPglucose synthesis
-
additional information
-
no activation by 3-phosphoglycerate; no activation by fructose 1,6-bisphosphate, fructose 6-phosphate, phosphoenolpyruvate or p-hydroxymandelonitrile-beta-D-glucopyranoside
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.09
alpha-D-galactose 1-phosphate
cosubstrate UTP, S0.5 value, hyperbolic behaviour, pH 8.0, 37°C
10
alpha-D-galactose 1-phosphate
-
pH 7.5, temperature not specified in the publication
0.031
alpha-D-glucose 1-phosphate
pH 7.5, temperature not specified in the publication
0.033
alpha-D-glucose 1-phosphate
-
pH 7.5, temperature not specified in the publication
0.055 - 0.08
alpha-D-glucose 1-phosphate
-
at physiological substrate concentration, pH 8.5, 37°C
0.122
alpha-D-glucose 1-phosphate
pH 7.2, temperature not specified in the publication, recombinant enzyme
0.13
alpha-D-glucose 1-phosphate
cosubstrate UTP, S0.5 value, hyperbolic behaviour, pH 8.0, 37°C
0.198
alpha-D-glucose 1-phosphate
pH 7.5, 37°C, recombinant mutant N491P/L492E
0.202
alpha-D-glucose 1-phosphate
pH 7.5, 37°C, recombinant mutant P414G/T415P
0.219
alpha-D-glucose 1-phosphate
pH 7.5, 37°C, recombinant mutant T406K/M407L
0.235
alpha-D-glucose 1-phosphate
pH 7.5, 37°C, recombinant mutant S309N/S311R
0.316
alpha-D-glucose 1-phosphate
pH 7.5, 37°C, recombinant enzyme
0.36
alpha-D-glucose 1-phosphate
cosubstrate TTP, S0.5 value, hyperbolic behaviour, pH 8.0, 37°C
0.68 - 1
alpha-D-glucose 1-phosphate
-
at substrate concentrations above 2 mM, pH 8.5, 37°C
0.68 - 1
alpha-D-glucose 1-phosphate
-
recombinant wild-type enzyme, pH 8.0, 25°C
0.715
alpha-D-glucose 1-phosphate
pH 7.5, 37°C, recombinant enzyme
0.83
alpha-D-glucose 1-phosphate
pH 7.5, 37°C, recombinant enzyme
0.11 - 0.13
diphosphate
-
at physiological substrate concentration, pH 8.5, 37°C
0.00167
UDP-glucose
pH 7.5, temperature not specified in the publication
0.00433
UDP-glucose
pH 7.5, temperature not specified in the publication
0.03
UDP-glucose
-
Ccut-8 mutant protein; K183A mutant protein; K332A mutant protein
0.12 - 0.18
UDP-glucose
-
at physiological substrate concentrations, pH 8.5, 37°C
0.774
UDP-glucose
pH 7.5, temperature not specified in the publication
0.053
UTP
pH 7.2, temperature not specified in the publication, recombinant enzyme
0.08
UTP
cosubstrate alpha-D-galactose 1-phosphate, S0.5 value, hyperbolic behaviour, pH 8.0, 37°C
additional information
additional information
-
kinetic parameters of various organisms, pH 8.0, overview
-
additional information
additional information
-
kinetic parameters of various organisms, pH 8.0, overview
-
additional information
additional information
-
kinetic parameters of various organisms, pH 8.0, overview
-
additional information
additional information
-
kinetic parameters of various organisms, pH 8.0, overview
-
additional information
additional information
-
kinetic parameters of various organisms, pH 8.0, overview
-
additional information
additional information
-
kinetic parameters of various organisms, pH 8.0, overview
-
additional information
additional information
-
kinetic parameters of various organisms, pH 8.0, overview
-
additional information
additional information
-
kinetic parameters of various organisms, pH 8.0, overview
-
additional information
additional information
-
kinetic parameters of various organisms, pH 8.0, overview
-
additional information
additional information
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
33.11
alpha-D-glucose 1-phosphate
pH 7.5, temperature not specified in the publication
0.21
UDP-glucose
pH 7.5, temperature not specified in the publication
19.98
UDP-glucose
pH 7.5, temperature not specified in the publication
19.98
UDP-glucose
pH 7.5, temperature not specified in the publication
additional information
additional information
-
-
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1067
alpha-D-glucose 1-phosphate
pH 7.5, temperature not specified in the publication
273
UDP-glucose
pH 7.5, temperature not specified in the publication
4610
UDP-glucose
pH 7.5, temperature not specified in the publication
11980
UDP-glucose
pH 7.5, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE