Information on EC 2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
2.7.7.9
-
RECOMMENDED NAME
GeneOntology No.
UTP-glucose-1-phosphate uridylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
show the reaction diagram
sequential ordered bi bi reaction mechanism
-
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
show the reaction diagram
sequential ordered bi bi reaction mechanism
-
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
show the reaction diagram
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
show the reaction diagram
sequential ordered bi bi reaction mechanism
-
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
show the reaction diagram
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
Q4QDU3
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
show the reaction diagram
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
-, O25363
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
Biosynthesis of secondary metabolites
-
chitin biosynthesis
-
Galactose metabolism
-
Metabolic pathways
-
Pentose and glucuronate interconversions
-
stachyose degradation
-
Starch and sucrose metabolism
-
sucrose biosynthesis II
-
sucrose degradation II (sucrose synthase)
-
UDP-glucose biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
UTP:alpha-D-glucose-1-phosphate uridylyltransferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glucose 1-phosphate uridylyltransferase
-
-
-
-
glucose-1-phosphate uridylyltransferase
-
-
-
-
glucose-1-phosphate uridylyltransferase
O25363
-
plastid UDP-glucose pyrophosphorylase
-
-
ST0452
Q975F9
locus name
ST0452
Sulfolobus tokodaii 7
Q975F9
locus name
-
UDP glucose pyrophosphorylase
-
-
-
-
UDP-Glc pyrophosphorylase
-
-
UDP-glucose pyrophosphorylase
-
-
-
-
UDP-glucose pyrophosphorylase
-
-
UDP-glucose pyrophosphorylase
P57751, Q9M9P3
-
UDP-glucose pyrophosphorylase
Arabidopsis thaliana Col-0
-
-
-
UDP-glucose pyrophosphorylase
Q9XUS5
-
UDP-glucose pyrophosphorylase
B8JMZ1
-
UDP-glucose pyrophosphorylase
A5XCL5
-
UDP-glucose pyrophosphorylase
O25363
-
UDP-glucose pyrophosphorylase
-
-
UDP-glucose pyrophosphorylase
Q16851
-
UDP-glucose pyrophosphorylase
-
-
UDP-glucose pyrophosphorylase
Q43772
-
UDP-glucose pyrophosphorylase
O05576
-
UDP-glucose pyrophosphorylase
Q9M4X0
-
UDP-glucose pyrophosphorylase
C7GP37
-
UDP-glucose pyrophosphorylase
Q8GQP8
-
UDP-glucose pyrophosphorylase
D3HTY9
-
UDP-glucose pyrophosphorylase
Trypanosoma brucei 427
D3HTY9
-
-
UDP-glucose pyrophosphorylase 1
-
-
UDP-glucose pyrophosphorylase 1
Arabidopsis thaliana Col-0
-
-
-
UDP-glucose pyrophosphorylase isoenzyme UGP5
-
-
UDP-glucose pyrophosphorylase UGP1
Q94B70
-
UDP-glucose pyrophosphorylase UGP2
P57751
-
UDP-glucose pyrophosphorylase UGP3
Q94B70
-
UDPG phosphorylase
-
-
-
-
UDPG pyrophosphorylase
-
-
-
-
UDPG-pyrophosphorylase
-
-
UDPG-pyrophosphorylase
Aureobasidium pullulans CJ001
-
-
-
UDPglucose pyrophosphorylase
-
-
-
-
UDPglucose pyrophosphorylase
Q4UVD0
-
UDPglucose pyrophosphorylase
Q8PK83
-
UGP
D3HTY9
-
UGP
Trypanosoma brucei 427
D3HTY9
-
-
UGP1
-
gene name
UGP1
Arabidopsis thaliana Col-0
-
gene name
-
UGPase
Q9XUS5
-
UGPase
B8JMZ1
-
UGPase
O25363
-
UGPase
Q16851
-
UGPase
-
-
UGPase
Q43772
-
UGPase
Q8GQP8
-
UGPG-PPase
-
-
uridine 5'-diphosphoglucose pyrophosphorylase
-
-
-
-
uridine diphosphate-D-glucose pyrophosphorylase
-
-
-
-
uridine diphosphate-glucose pyrophosphorylase
-
-
uridine diphosphate-glucose pyrophosphorylase
Q8GQP9
-
uridine diphosphoglucose pyrophosphorylase
-
-
-
-
uridine-diphosphate glucose pyrophosphorylase
-
-
-
-
uridylyltransferase, glucose 1-phosphate
-
-
-
-
UTP:glucose-1-phosphate uridylyltransferase
-
-
VldB
Streptomyces hygroscopicus KCCM 11405
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9026-22-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Acanthamoeba castellanii NEFF
Neff
-
-
Manually annotated by BRENDA team
Acetabularia sp.
-
-
-
Manually annotated by BRENDA team
ecotype Columbia for wild-type, ecotype Bensheim for transgenic plants; gene Ugp, inducible by exogenous sucrose, light and cold stress
-
-
Manually annotated by BRENDA team
syncytia induced by nematode Heterodera schachtii
UniProt
Manually annotated by BRENDA team
var. Landsberg erecta, gene UGP1, a sucrose-induced gene
-
-
Manually annotated by BRENDA team
wild type, Pi-deficient mutant, Pi-excess mutant
-
-
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
var. Landsberg erecta, gene UGP1, a sucrose-induced gene
-
-
Manually annotated by BRENDA team
isolated from sea mud
-
-
Manually annotated by BRENDA team
Aureobasidium pullulans CJ001
isolated from sea mud
-
-
Manually annotated by BRENDA team
Beta vulgaris subsp. vulgaris var. altissima
sugar beet
-
-
Manually annotated by BRENDA team
cow
-
-
Manually annotated by BRENDA team
crystallized liver enzyme
-
-
Manually annotated by BRENDA team
male calf
-
-
Manually annotated by BRENDA team
pigeon
-
-
Manually annotated by BRENDA team
in addition to UGPase, presence of dual substrate UDP-hexose pyrophosphorylase
SwissProt
Manually annotated by BRENDA team
cv. Calypiso
-
-
Manually annotated by BRENDA team
several mutant strains, some derived from wild-type parent strain AB1133
-
-
Manually annotated by BRENDA team
Golgi apparatus and cytosolic isozyme
-
-
Manually annotated by BRENDA team
gene galU
UniProt
Manually annotated by BRENDA team
strain 26 695
-
-
Manually annotated by BRENDA team
Helicobacter pylori 26 695
strain 26 695
-
-
Manually annotated by BRENDA team
crystallized liver enzyme
-
-
Manually annotated by BRENDA team
isoform II
UniProt
Manually annotated by BRENDA team
gene Ugp
SwissProt
Manually annotated by BRENDA team
transgenes PPL-1 and PPL-2
-
-
Manually annotated by BRENDA team
crystallized liver enzyme
-
-
Manually annotated by BRENDA team
gene OsUgp2
UniProt
Manually annotated by BRENDA team
isoform Ugp1
Uniprot
Manually annotated by BRENDA team
isoforms Ugp1 and Ugp2
Uniprot
Manually annotated by BRENDA team
lamb
-
-
Manually annotated by BRENDA team
different isoforms in different tissues
-
-
Manually annotated by BRENDA team
commercial product
-
-
Manually annotated by BRENDA team
gene UGP1, i.e. open reading frame YKL248
-
-
Manually annotated by BRENDA team
isoform Ugp1
-
-
Manually annotated by BRENDA team
Saccharomyces fragilis
galactose-adopted
-
-
Manually annotated by BRENDA team
cv. Norchip
-
-
Manually annotated by BRENDA team
cv. Snowden MTs
-
-
Manually annotated by BRENDA team
cv. Rox Orange
-
-
Manually annotated by BRENDA team
ATCC 31461
-
-
Manually annotated by BRENDA team
strain ATCC 31461
-
-
Manually annotated by BRENDA team
subsp. zooepidemicus. i.e. Streptococcus zooepidemicus
UniProt
Manually annotated by BRENDA team
strain KCCM 11405, recombinant protein. Enzyme is part of the validamycin A biosynthetic pathway
-
-
Manually annotated by BRENDA team
Streptomyces hygroscopicus KCCM 11405
strain KCCM 11405, recombinant protein. Enzyme is part of the validamycin A biosynthetic pathway
-
-
Manually annotated by BRENDA team
Streptomyces thermophilus LY03
strain LY03
-
-
Manually annotated by BRENDA team
Sulfolobus tokodaii 7
-
SwissProt
Manually annotated by BRENDA team
wild-type and mutant RN-
-
-
Manually annotated by BRENDA team
Trypanosoma brucei 427
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
evolution
-
the plant UGPases belongs to the so called UGPase-A family
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
-
involved in sulfolipid synthesis
metabolism
O05576
involved in cell envelope precursor synthesis
metabolism
-
UDPG-pyrophosphorylase is the key enzyme involved in pullulan biosynthesis and pullulan production by Aureobasidium pullulans
metabolism
D3HTY9, -
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
Arabidopsis thaliana Col-0
-
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
Aureobasidium pullulans CJ001
-
UDPG-pyrophosphorylase is the key enzyme involved in pullulan biosynthesis and pullulan production by Aureobasidium pullulans
-
physiological function
C7GP37
the enzyme is essential for survival
physiological function
D3HTY9, -
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
Q8GQP8, -
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
Q9M4X0
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
-, O25363
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
Arabidopsis thaliana Col-0
-
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
Trypanosoma brucei 427
-
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
-
metabolism
Trypanosoma brucei 427
-
the enzyme catalyzes the last and reversible step of the de novo UDP-Glc biosynthetic pathway
-
additional information
Q16851
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
C7GP37
structure comparison of human and yeast enzyme, overview
additional information
D3HTY9, -
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
Q8GQP8, -
structure-function analysis, homology modeling
additional information
-, O25363
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
Trypanosoma brucei 427
-
UDP-Glc is bound in a deep cleft located at the center of the catalytic domain that consists of highly conserved residues
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
show the reaction diagram
-
13.7% of the activity with UTP
-
r
diphosphate + CDP-glucose
CTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
no activity
-
-
-
diphosphate + CDP-glucose
CTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
no activity
-
-
-
diphosphate + CDP-glucose
CTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
calf and human liver, poor substrate
-
r
diphosphate + CDP-glucose
CTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
very low activity, wild-type and mutant W218
-
r
diphosphate + CDP-glucose
CTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
18.5% of the activity with UTP
-
r
diphosphate + GDP-glucose
GTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
no activity
-
-
-
diphosphate + GDP-glucose
GTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
no activity
-
-
-
diphosphate + GDP-glucose
GTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
calf and human liver, poor substrate
-
-
r
diphosphate + GDP-glucose
GTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
14.3% of the activity with UTP
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
?
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
no activity
-
-
-
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
poor substrate
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
poor substrate
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
poor substrate
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
poor substrate
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
poor substrate
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
poor substrate
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
poor substrate
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
poor substrate
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
calf and human liver
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
very low activity, wild-type and mutant W218
-
r
diphosphate + UDP-galactose
UTP + alpha-D-galactose 1-phosphate
show the reaction diagram
Q19TV8
-
-
-
r
diphosphate + UDP-glucose
UTP + alpha-D-glucose 1-phosphate
show the reaction diagram
-, Q4QDU3
-
-
-
r
diphosphate + UDP-glucose
UTP + alpha-D-glucose 1-phosphate
show the reaction diagram
Q19TV8
-
-
-
r
diphosphate + UDP-mannose
UTP + D-mannose 1-phosphate
show the reaction diagram
-
calf and human liver, poor substrate
-
-
r
diphosphate + UDP-xylose
UTP + D-xylose 1-phosphate
show the reaction diagram
-
-
-
-
r
diphosphate + UDP-xylose
UTP + D-xylose 1-phosphate
show the reaction diagram
-
poor substrate
-
-
r
diphosphate + UDP-xylose
UTP + D-xylose 1-phosphate
show the reaction diagram
-
poor substrate
-
-
r
diphosphate + UDP-xylose
UTP + D-xylose 1-phosphate
show the reaction diagram
-
poor substrate
-
-
r
diphosphate + UDP-xylose
UTP + D-xylose 1-phosphate
show the reaction diagram
-
calf and human liver
-
-
r
diphosphate + UDP-xylose
UTP + D-xylose 1-phosphate
show the reaction diagram
-
reaction at 10% the rate of UDP-glucose or UDP-galactose pyrophosphorolysis
-
-
r
farnesyl triphosphate + UDP-glucose
farnesyl-tetraphosphouridine + alpha-D-glucose + diphosphate
show the reaction diagram
-
-
-
-
?
geranyl triphosphate + UDP-glucose
geranyl-tetraphosphouridine + alpha-D-glucose + diphosphate
show the reaction diagram
-
-
-
-
?
isopentenyl triphosphate + UDP-glucose
isopentenyl-tetraphosphouridine + alpha-D-glucose + diphosphate
show the reaction diagram
-
-
-
-
?
methylenebisphosphonate + UDP-glucose
uridine 5-(beta,gamma-methylenetriphosphate) + alpha-D-glucose + diphosphate
show the reaction diagram
-
-
-
-
?
TTP + alpha-D-glucose 1-phosphate
TDP-glucose + diphosphate
show the reaction diagram
Q4UVD0
-
-
-
r
TTP + alpha-D-glucose 1-phosphate
TDP-glucose + diphosphate
show the reaction diagram
Q8PK83
-
-
-
r
UDP-glucose + adenosine 5'-tetraphosphate
D-glucose-1-phosphate + adenosyl-5'-pentaphospho-5'-uridine
show the reaction diagram
-
-
-
-
?
UDP-glucose + ATP
D-glucose-1-phosphate + adenosyl-5'-tetraphospho-5'-uridine
show the reaction diagram
-
-
-
-
?
UDP-glucose + CTP
D-glucose-1-phosphate + cytidinyl-5'-tetraphospho-5'-uridine
show the reaction diagram
-
-
-
-
?
UDP-glucose + GTP
D-glucose-1-phosphate + guanosyl-5'-tetraphospho-5'-uridine
show the reaction diagram
-
-
-
-
?
UDP-glucose + guanosine 5'-tetraphosphate
D-glucose-1-phosphate + guanosyl-5'-pentaphospho-5'-uridine
show the reaction diagram
-
-
-
-
?
UDP-glucose + tetrapolyphosphate
uridine-5'-pentaphosphate + D-glucose-1-phosphate
show the reaction diagram
-
-
-
-
?
UDP-glucose + tripolyphosphate
uridine-5'-tetraphosphate + D-glucose-1-phosphate
show the reaction diagram
-
-
-
-
?
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
show the reaction diagram
-
-
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
show the reaction diagram
-
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
show the reaction diagram
-
-
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
show the reaction diagram
-
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
show the reaction diagram
-
no activity
-
-
-
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
show the reaction diagram
-
no activity
-
-
-
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
show the reaction diagram
-
low activity
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
show the reaction diagram
-
about 15% of the activity with UDP-glucose
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
show the reaction diagram
-
equilibrium dialysis: 8 mol UDP-galactose bound per mol enzyme, 3.5% of the activity with UDP-glucose
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
show the reaction diagram
-
reverse reaction: calf and human liver
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
show the reaction diagram
-
at the same rate as UDP-glucose
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
show the reaction diagram
-
reaction at 5% the rate of UDP-glucose synthesis
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
show the reaction diagram
-
1-12% of the activity with UDP-glucose
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
Saccharomyces fragilis
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
Columba sp., Acetabularia sp., Beta vulgaris subsp. vulgaris var. altissima
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
Q43772
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-, Q43772
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-, Q4QDU3
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
Q19TV8
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
O05576
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
D3HTY9, -
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
Q8GQP8, -
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-, O25363
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
Q16851
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
C7GP37
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
A5XCL5
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
B8JMZ1
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
Q9XUS5
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
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
show the reaction diagram
-
specific for alpha-D-glucose 1-phosphate
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
specific for alpha-D-glucose 1-phosphate
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
specific for alpha-D-glucose 1-phosphate
specific for UDP-glucose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
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
show the reaction diagram
-
highly specific for UTP
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
highly specific for UTP
specific for UDP-glucose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
highly specific for UTP
specific for UDP-glucose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
highly specific for UTP
specific for UDP-glucose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
reverse reaction: highly specific for UDP-glucose
specific for UDP-glucose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
reverse reaction: highly specific for UDP-glucose
specific for UDP-glucose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
reverse reaction: highly specific for UDP-glucose
specific for UDP-glucose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
reaction at the same rate as UDP-galactose
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
equilibrium dialysis: 8 mol UDP-glucose bound per mol enzyme
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
reaction critical to mono- and polysaccharide biosynthesis
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
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
show the reaction diagram
-
central reaction in galactose and trehalose metabolism
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
enzyme is induced during amoeba encystment
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
enzyme is essential for cell viability
-
-
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
involved in exopolysaccharide biosynthesis
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-, Q43772
key enzyme in biosynthesis of sucrose, cellulose, and other saccharides
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
enzyme is specific for UTP
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
Sulfolobus tokodaii, Sulfolobus tokodaii 7
Q975F9
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
show the reaction diagram
Streptomyces thermophilus LY03
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
Streptomyces thermophilus LY03
-
involved in exopolysaccharide biosynthesis
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
Trypanosoma brucei 427
D3HTY9
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
Streptomyces hygroscopicus KCCM 11405
-
enzyme is specific for UTP
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
Acanthamoeba castellanii NEFF
-
highly specific for UTP, reverse reaction: highly specific for UDP-glucose
specific for UDP-glucose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
Acanthamoeba castellanii NEFF
-
enzyme is induced during amoeba encystment
-
r
UTP + alpha-D-glucose 1-phosphate
UDP-glucose + diphosphate
show the reaction diagram
P57751
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
UDP-glucose + diphosphate
show the reaction diagram
-
14.2% activity with galactose-1-phosphate
-
-
?
UTP + alpha-D-glucose 1-phosphate
UDP-glucose + diphosphate
show the reaction diagram
Q4UVD0
in the presence of a divalent metal cation (mainly Mg2+)
-
-
r
UTP + alpha-D-glucose 1-phosphate
UDP-glucose + diphosphate
show the reaction diagram
Q8PK83
in the presence of a divalent metal cation (mainly Mg2+)
-
-
r
UTP + D-glucose-1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
-
?
UTP + D-glucose-1-phosphate
UDP-glucose + diphosphate
show the reaction diagram
-
-
-
-
?
UTP + D-glucose-1-phosphate
UDP-glucose + diphosphate
show the reaction diagram
-
-
-
-
?
UTP + D-glucose-1-phosphate
UDP-glucose + diphosphate
show the reaction diagram
-
-
-
-
r
UTP + D-glucose-1-phosphate
UDP-glucose + diphosphate
show the reaction diagram
-
-
-
-
?
UTP + glucose-1-phosphate
UDP-glucose + diphosphate
show the reaction diagram
-
-
-
-
?
monothiodiphosphate + UDP-glucose
UTPbeta,gammaS + alpha-D-glucose 1-phosphate
show the reaction diagram
-
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 25C: 0.5 min
ir
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
no activity with ADP-glucose
-
-
-
additional information
?
-
-
no activity with ADP-glucose
-
-
-
additional information
?
-
-
no activity with ADP-glucose
-
-
-
additional information
?
-
-
no activity with ATP, CTP, and GTP
-
-
-
additional information
?
-
-
no activity with ATP, CTP, and GTP
-
-
-
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
?
-
-
no activity with TPP
-
-
-
additional information
?
-
-
TTP is a poor substrate
-
-
-
additional information
?
-
-
regulation
-
-
-
additional information
?
-
-
involved in synthesis of hemagglutinin, sulfated proteoglycans, and glycogen in cartilage
-
-
-
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
?
-
A3QQQ3
isoform Ugp1 is required for callose deposition during pollen mother cell meiosis and bridges the apoplastic unloading pathway and pollen development
-
-
-
additional information
?
-
-, Q4QDU3
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
?
-
Q19TV8
no substrate: alpha-D-glalctose 1-phosphate
-
-
-
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
?
-
-
the enzyme catalyses a freely reversible reaction and is specific for alpha-D-glucose 1-phosphate
-
-
-
additional information
?
-
D3HTY9, -
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
?
-
Trypanosoma brucei 427
D3HTY9
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
?
-
Acanthamoeba castellanii NEFF
-
no activity with ADP-glucose, no activity with ATP, CTP, and GTP
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
D3HTY9, -
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
Q8GQP8, -
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-, O25363
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
Q16851
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
C7GP37
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
A5XCL5
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
B8JMZ1
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
Q9XUS5
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
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
show the reaction diagram
-
reaction critical to mono- and polysaccharide biosynthesis
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
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
show the reaction diagram
-
central reaction in galactose and trehalose metabolism
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
enzyme is induced during amoeba encystment
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
enzyme is essential for cell viability
-
-
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
involved in exopolysaccharide biosynthesis
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-, Q43772
key enzyme in biosynthesis of sucrose, cellulose, and other saccharides
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
Streptomyces thermophilus LY03
-
involved in exopolysaccharide biosynthesis
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
Trypanosoma brucei 427
D3HTY9
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
Acanthamoeba castellanii NEFF
-
enzyme is induced during amoeba encystment
-
r
additional information
?
-
-
regulation
-
-
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
28% as effective as Mg2+ at 1 mM; activation
Ca2+
-
16% as effective as Mg2+ at 2 mM; activation
Ca2+
-
50% as effective as Mg2+ at 1 mM; activation
Ca2+
-
activation
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+
-
75% activity at 2 mM; activation
Co2+
-
47-49% activity at 2 mM; activation
Co2+
-
activation; Co2+ in excess of diphosphate-concentration inhibits
Co2+
-
activation
Co2+
D3HTY9, -
activates
Magnesium
-, Q6M6R3
crystallization data, two magnesium ions coordinate to UDP-glucose. Magnesium is involved in catalytic mechanism
Mg2+
-
requirement
Mg2+
-
requirement
Mg2+
-
6-8fold increase in activity; activation; requirement
Mg2+
-
activation
Mg2+
-
activation; requirement
Mg2+
-
activation
Mg2+
-
-
Mg2+
-
activation
Mg2+
-
Mg-diphosphate is the actual substrate; MgUTP is the actual substrate; requirement
Mg2+
-
5 mM; requirement
Mg2+
-
increasing MgSO4 concentrations shift the apparent equilibrium toward UDP-glucose synthesis; Mg-diphosphate is the actual substrate; requirement
Mg2+
-
Mg-diphosphate is the actual substrate; MgUTP is the actual substrate; requirement
Mg2+
Acetabularia sp., Beta vulgaris subsp. vulgaris var. altissima, Bombyx mori
-
requirement
Mg2+
-
requirement
Mg2+
-
requirement
Mg2+
-
requirement
Mg2+
-
absolute requirement for activity
Mg2+
O05576
absolutely required
Mg2+
D3HTY9, -
required, best at 10 mM
Mg2+
-
required
Mg2+
-, O25363
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
Mn2+
-
6-8fold increase in activity; activation
Mn2+
-
activation
Mn2+
-
maximal activity at 1 mM
Mn2+
-
-
Mn2+
-
maximal activity at 1 mM
Mn2+
-
about 25% as effective as Mg2+; activation; UDP-glucose synthesis: Mn2+ in excess of diphosphate-concentration inhibits
Ni2+
-
highly stimulatory
Ni2+
-
no effect
Mn2+
D3HTY9, -
activates
additional information
-
requirement for divalent cations
additional information
-
requirement for divalent cations
additional information
-
requirement for divalent cations
additional information
-
requirement for divalent cations
additional information
D3HTY9, -
the enzyme is divalent cation-dependent, no activation by Zn2+ and Cu2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-phosphoglycerate
-
no inhibition of UDP-glucose synthesis
alpha-D-galactose 1-phosphate
-
-
alpha-D-galactose 1-phosphate
-
no inhibition
alpha-D-galactose 1-phosphate
-
-
alpha-D-galactose 1-phosphate
-
competitive
alpha-D-galactose 1-phosphate
-
at high concentrations
alpha-D-galactose 1-phosphate
-
-
alpha-D-glucose 1-phosphate
-
UDP-glucose pyrophosphorolysis
alpha-D-glucose 1-phosphate
-
product inhibition
alpha-D-glucose 1-phosphate
-
product inhibition
alpha-D-glucose 1-phosphate
-
product inhibition
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
D-fructose 2,6-bisphosphate
-
no inhibition of UDP-glucose synthesis
D-fructose 6-phosphate
-
-
D-galactosamine
-
-
D-galactose 6-phosphate
-
UDP-glucose pyrophosphorolysis
diphosphate
-
product inhibition
diphosphate
-
possible alternate regulatory mechanism; product inhibition
diphosphate
-
product inhibition
diphosphate
-
noncompetitive to glucose 1-phosphate and UTP
diphosphate
-
with 0.25 mM 57% activity, with 1 mM 11% activity, with 10 mM 1.5% activity
iodoacetamide
-
wild-type: loss of 56% activity after 30 min at 0.1 mM, mutant C123S is not affected
Mg-diphosphate
-
product inhibition
Mg-diphosphate
-
product inhibition
MgUTP
-
wild-type and mutants C123S, H266R, W218, R389H, R422Q, R445H
MgUTP2-
-
-
phosphate
-
-
phosphate
-
noncompetitive to glucose 1-phosphate and UTP
Sucrose
-
54% inhibition at 2%
TDP-glucose
-
-
TDP-rhamnose
-
-
UDP-D-mannose
-
-
UDP-D-mannose
-
-
UDP-galactose
-
UDP-glucose pyrophosphorolysis
UDP-galactose
-
-
UDP-galactose
-
14% inhibition at 0.35 mM
UDP-galactose
-
strong inhibition
UDP-galactose
-
competitive
UDP-galacturonic acid
-
-
UDP-galacturonic acid
-
48% inhibition at 0.43 m
UDP-glucose
-
UDP-galactose pyrophosphorolysis or UDP-glucose synthesis
UDP-glucose
-
product inhibition
UDP-glucose
-
87% inhibition at 0.08 mM
UDP-glucose
-
product inhibition
UDP-glucose
-
competitive to UTP, noncompetitive to glucose 1-phosphate
UDP-glucuronic acid
-
-
UDP-glucuronic acid
-
56% inhibition at 0.45 mM
UDP-mannose
-
23% inhibition at 0.45 mM
UDP-xylose
-
32% inhibition at 0.36 mM
UTP
-
UDP-glucose pyrophosphorolysis
UTP
-
MgUTP2-
UTP
-
product inhibition
UTP
-
product inhibition
UTP
-
competitive to UDP-glucose; product inhibition
Mn2+
-
in excess of diphosphate-concentration, activates at lower concentrations
additional information
-
product inhibition pattern
-
additional information
-
inhibition kinetics for UDP-sugars
-
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: Tween-20
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
no activation
2-mercaptoethanol
-
-
2-mercaptoethanol
-
-
2-mercaptoethanol
-
requirement
2-mercaptoethanol
-
-
3-phosphoglycerate
-
slight activation
Co2+
-
no effect on liver enzyme form I, 2fold activation of enzyme form from sublingual gland, inhibition of enzyme form from submandibular gland
D-erythrose 4-phosphate
-
slight activation
D-fructose 6-phosphate
-
slight activation
dithiothreitol
-
increases wild-type activity by about 25%
Sucrose
-
activates; inducible by
Triton X-100
-
activation, only membrane-bound Golgi-enzyme
DTT
-
requirement
additional information
-
no effect of PCMB, iodoacetate, 2-mercaptoethanol or DTT
-
additional information
-
no activation by 3-phosphoglycerate
-
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
-
additional information
-
-
-
additional information
-
rat mammary gland enzyme seems to undergo structural changes that lead to a more active form
-
additional information
-
enzyme expression is inducible by exogenous sucrose, light and cold stress
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
10
-
alpha-D-galactose 1-phosphate
-
pH 7.5, temperature not specified in the publication
0.01
-
alpha-D-glucose 1-phosphate
-
pH 7.8, 37C
0.03
0.048
alpha-D-glucose 1-phosphate
-
pH 7.5, 30C
0.03
0.048
alpha-D-glucose 1-phosphate
-
-
0.03
0.048
alpha-D-glucose 1-phosphate
-
pH 7.8
0.03
0.048
alpha-D-glucose 1-phosphate
-
pH 8.5, 37C
0.033
-
alpha-D-glucose 1-phosphate
-
pH 7.5, temperature not specified in the publication
0.0364
-
alpha-D-glucose 1-phosphate
Q8GQP8, -
pH 7.5, 37C
0.04455
-
alpha-D-glucose 1-phosphate
O05576
-
0.055
0.08
alpha-D-glucose 1-phosphate
-
-
0.055
0.08
alpha-D-glucose 1-phosphate
-
pH 7.8
0.055
0.08
alpha-D-glucose 1-phosphate
-
at physiological substrate concentration, pH 8.5, 37C
0.06
-
alpha-D-glucose 1-phosphate
Q4UVD0
-
0.067
-
alpha-D-glucose 1-phosphate
Q16851
pH 7.5, 37C, recombinant mutant E412K
0.074
-
alpha-D-glucose 1-phosphate
-
pH 8.35,25C
0.095
-
alpha-D-glucose 1-phosphate
-
-
0.095
-
alpha-D-glucose 1-phosphate
-
pH 7.8
0.122
-
alpha-D-glucose 1-phosphate
D3HTY9, -
pH 7.2, temperature not specified in the publication, recombinant enzyme
0.14
0.18
alpha-D-glucose 1-phosphate
-
pH 8.0, 30C
0.14
0.18
alpha-D-glucose 1-phosphate
-
-
0.14
-
alpha-D-glucose 1-phosphate
-
UDP-glucose synthesis
0.151
-
alpha-D-glucose 1-phosphate
Q16851
pH 7.5, 37C, recombinant mutant K410S
0.155
-
alpha-D-glucose 1-phosphate
Q16851
pH 7.5, 37C, recombinant mutant E412Q
0.183
-
alpha-D-glucose 1-phosphate
B8JMZ1
pH 7.5, 37C, recombinant enzyme
0.192
-
alpha-D-glucose 1-phosphate
Q4QDU3
pH 7.8, 25C
0.198
-
alpha-D-glucose 1-phosphate
Q16851
pH 7.5, 37C, recombinant mutant N491P/L492E
0.202
-
alpha-D-glucose 1-phosphate
Q16851
pH 7.5, 37C, recombinant mutant P414G/T415P
0.205
-
alpha-D-glucose 1-phosphate
Q16851
pH 7.5, 37C, recombinant mutant E412D
0.217
-
alpha-D-glucose 1-phosphate
Q16851
pH 7.5, 37C, recombinant mutant V416N
0.219
-
alpha-D-glucose 1-phosphate
Q16851
pH 7.5, 37C, recombinant mutant T406K/M407L
0.235
-
alpha-D-glucose 1-phosphate
Q16851
pH 7.5, 37C, recombinant mutant S309N/S311R
0.24
-
alpha-D-glucose 1-phosphate
Q19TV8
pH 7.5, 30C
0.24
-
alpha-D-glucose 1-phosphate
-
-
0.253
-
alpha-D-glucose 1-phosphate
Q16851
pH 7.5, 37C, recombinant enzyme
0.316
-
alpha-D-glucose 1-phosphate
A5XCL5
pH 7.5, 37C, recombinant enzyme
0.36
-
alpha-D-glucose 1-phosphate
-
UDP-glucose synthesis
0.46
-
alpha-D-glucose 1-phosphate
-
-
0.68
1
alpha-D-glucose 1-phosphate
-
pH 7.2, 30C
0.68
1
alpha-D-glucose 1-phosphate
-
at substrate concentrations above 2 mM, pH 8.5, 37C
0.68
1
alpha-D-glucose 1-phosphate
-
pH 8.0, 37C
0.68
1
alpha-D-glucose 1-phosphate
-
recombinant wild-type enzyme, pH 8.0, 25C
0.715
-
alpha-D-glucose 1-phosphate
Q9XUS5
pH 7.5, 37C, recombinant enzyme
0.83
-
alpha-D-glucose 1-phosphate
-
UDP-glucose synthesis
0.83
-
alpha-D-glucose 1-phosphate
C7GP37
pH 7.5, 37C, recombinant enzyme
0.19
-
D-glucose-1-phosphate
-
-
0.83
-
D-glucose-1-phosphate
-
-
0.027
-
diphosphate
-
Y192A mutant protein
0.03
-
diphosphate
-
pyrophosphorolysis
0.03
-
diphosphate
-
Ccut-8 mutant protein; K183A mutant protein
0.034
-
diphosphate
Q43772
recombinant wild-type, pH 7.6, 25C
0.039
-
diphosphate
-
wild-type protein
0.04
-
diphosphate
-
K332A mutant protein
0.054
-
diphosphate
-
pH 8.5, 37C
0.07
-
diphosphate
-
pyrophosphorolysis
0.084
-
diphosphate
-
-
0.084
-
diphosphate
-
pH 7.8
0.09
-
diphosphate
-
Ncut-21 mutant protein
0.11
0.13
diphosphate
-
pH 8.0, 30C
0.11
0.13
diphosphate
-
at physiological substrate concentration, pH 8.5, 37C
0.115
-
diphosphate
-
-
0.17
-
diphosphate
-
pH 8.35, 25C
0.18
-
diphosphate
-
non-galactosemic phenotype, pH 7.8, 37C
0.2
-
diphosphate
-
galactosemic phenotype, pH 7.8, 37C
0.2
-
diphosphate
Q4QDU3
pH 7.8, 25C
0.21
-
diphosphate
-
-
0.21
-
diphosphate
-
pH 7.8
0.24
-
diphosphate
-
K405A mutant protein
0.26
-
diphosphate
-
-
0.407
-
diphosphate
Q43772
recombinant mutant C99S, pH 7.6, 25C
0.9
-
diphosphate
-
Ncut-37 mutant protein
2.4
-
diphosphate
-
pH 7.6, 37C
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
0.32
-
farnesyl triphosphate
-
pH 8.0, 30C
0.21
-
geranyl triphosphate
-
pH 8.0, 30C
0.51
-
isopentenyl triphosphate
-
pH 8.0, 30C
1.1
-
methylenebisphosphonate
-
pH 8.0, 30C
-
0.33
-
Mg-diphosphate
-
pH 7.2, 30C
0.56
-
Mg-diphosphate
-
pyrophosphorolysis
0.22
-
Mg-UTP
-
UDP-glucose synthesis
0.58
-
Mg2+
Q4UVD0
pyrophosphorolysis direction
4.5
-
tripolyphosphate
-
30C, pH 8.0
0.35
-
TTP
Q8PK83
-
2
-
TTP
-
pH 7.8, 37C
0.26
-
UDP-galactose
Q19TV8
pH 7.5, 30C
0.42
-
UDP-galactose
-
pH 7.8
0.03
-
UDP-glucose
-
Ccut-8 mutant protein; K183A mutant protein; K332A mutant protein
0.031
-
UDP-glucose
-
Y192A mutant protein
0.034
-
UDP-glucose
-
wild-type protein
0.035
-
UDP-glucose
-
30C, pH 8.0
0.04
-
UDP-glucose
-
pyrophosphorolysis
0.04
-
UDP-glucose
-
K405A mutant protein
0.05
0.066
UDP-glucose
-
-
0.05
0.066
UDP-glucose
-
pH 7.8
0.05
0.066
UDP-glucose
-
-
0.05
0.066
UDP-glucose
-
pH 7.6, 37C
0.06
-
UDP-glucose
-
pyrophosphorolysis
0.065
-
UDP-glucose
Q43772
recombinant wild-type, pH 7.6, 25C
0.074
-
UDP-glucose
-
K260A mutant protein
0.101
-
UDP-glucose
Q43772
recombinant mutant C99S, pH 7.6, 25C
0.105
-
UDP-glucose
Q4QDU3
pH 7.8, 25C
0.11
-
UDP-glucose
Q19TV8
pH 7.5, 30C
0.118
-
UDP-glucose
-
Ccut-101 mutant protein
0.12
0.18
UDP-glucose
-
pH 8.0, 30C
0.12
0.18
UDP-glucose
-
at physiological substrate concentrations, pH 8.5, 37C
0.14
-
UDP-glucose
-
non-galactosemic phenotype, pH 7.8, 37C
0.18
-
UDP-glucose
-
galactosemic phenotype, pH 7.8, 37C
0.19
-
UDP-glucose
-
pH 8.35, 25C
0.31
-
UDP-glucose
-
Ccut-32 mutant protein
0.362
-
UDP-glucose
-
Ccut-67 mutant protein
0.4
-
UDP-glucose
-
-
0.503
-
UDP-glucose
-
Delta 1-8 mutant protein
0.555
-
UDP-glucose
-
Delta 1-4 mutant protein
0.68
-
UDP-glucose
-
pyrophosphorolysis
1.1
-
UDP-glucose
-
Ncut-21 mutant protein
57
-
UDP-glucose
-
Ncut-37 mutant protein
0.0075
-
UTP
-
isoenzyme UgpG, 30C, pH 7.8
0.0085
-
UTP
Q8GQP8, -
pH 7.5, 37C
0.025
-
UTP
-
pH 7.5, temperature not specified in the publication
0.03
-
UTP
-
pH 8.5, 37C
0.048
-
UTP
-
liver
0.048
-
UTP
-
pH 7.8
0.048
-
UTP
-
liver
0.053
-
UTP
D3HTY9, -
pH 7.2, temperature not specified in the publication, recombinant enzyme
0.058
0.07
UTP
-
pH 7.8, 37C
0.058
0.07
UTP
-
pH 8.0, 37C
0.07
-
UTP
Q4QDU3
pH 7.8, 25C
0.08
-
UTP
-
UDP-glucose synthesis
0.093
-
UTP
-
pH 8.35, 25C
0.1
0.2
UTP
-
pH 7.5, 30C
0.1
0.2
UTP
-
pH 8.0, 30C
0.1
0.2
UTP
-
at physiological substrate concentrations, pH 8.5, 37C
0.11
-
UTP
Q8PK83
-
0.17
-
UTP
-
UDP-glucose synthesis
0.229
-
UTP
-
isoenzyme RmlA, 30C, pH 7.8
0.32
-
UTP
-
pH 7.2, 30C
0.53
-
UTP
-
at substrate concentrations above 2 mM, pH 8.5, 37C
0.56
-
MgUTP
-
recombinant wild-type enzyme, pH 8.0, 25C
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
two-substrate kinetics
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
D3HTY9, -
Michaelis-Menten kinetics, overview
-
additional information
-
additional information
-
kinetics, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
48.81
-
alpha-D-glucose 1-phosphate
Q8GQP8, -
pH 7.5, 37C
55.03
-
alpha-D-glucose 1-phosphate
O05576
-
0.033
-
farnesyl triphosphate
-
pH 8.0, 30C
0.038
-
geranyl triphosphate
-
pH 8.0, 30C
0.013
-
isopentenyl triphosphate
-
pH 8.0, 30C
10
-
TTP
Q8PK83
-
29.3
-
UTP
Q8PK83
-
69.05
-
UTP
Q8GQP8, -
pH 7.5, 37C
27
-
methylenebisphosphonate
-
pH 8.0, 30C
-
additional information
-
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1240
-
alpha-D-glucose 1-phosphate
O05576
-
6756
0.103
-
farnesyl triphosphate
-
pH 8.0, 30C
21070
0.181
-
geranyl triphosphate
-
pH 8.0, 30C
302713
0.025
-
isopentenyl triphosphate
-
pH 8.0, 30C
302712
24.55
-
methylenebisphosphonate
-
pH 8.0, 30C
0
18.3
-
TTP
Q4UVD0
-
17549
28.3
-
TTP
Q8PK83
-
17549
183.3
-
UTP
Q4UVD0
-
17783
266.7
-
UTP
Q8PK83
-
17783
7870
-
UTP
O05576
-
17783
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.135
-
alpha-D-glucose 1-phosphate
-
pH 8.0, 30C
0.213
-
diphosphate
-
versus glucose 1-phosphate, pH 8.35, 25C
0.95
-
diphosphate
-
versus UTP, pH 8.35, 25C
0.095
-
MgUTP2-
-
mutant H266R, pH 8.0, 25C
10.9
-
phosphate
-
versus UTP, pH 8.35, 25C
12.2
-
phosphate
-
versus glucose 1-phosphate, pH 8.35, 25C
4.8
-
UDP-D-galactose
-
-
4.8
-
UDP-D-galactose
-
pH 7.5, 30C
0.21
-
UDP-D-galacturonic acid
-
pH 7.5, 30C
0.93
-
UDP-D-galacturonic acid
-
-
0.005
-
UDP-D-glucose
-
pH 7.5, 30C
0.05
-
UDP-D-glucose
-
pH 8.5, 37C
0.13
-
UDP-D-glucose
-
-
0.15
-
UDP-D-glucuronic acid
-
pH 7.5, 30C
0.75
-
UDP-D-glucuronic acid
-
-
9.6
-
UDP-D-mannose
-
-
9.6
-
UDP-D-mannose
-
pH 7.5, 30C
0.24
-
UDP-D-xylose
-
pH 7.5, 30C
1.6
-
UDP-D-xylose
-
-
0.015
-
UDP-glucose
-
versus glucose 1-phosphate, pH 8.35, 25C
0.12
-
UDP-glucose
-
versus UTP, pH 8.35, 25C
0.104
-
UTP
-
pH 8.5, 37C
0.17
-
UTP
-
versus UDP-glucose, pH 8.35, 25C
0.42
-
MgUTP2-
-
pH 8.0, 30C
additional information
-
additional information
-
simple additive inhibition of inhibitors at low individual concentrations and low substrate concentrations
-
additional information
-
additional information
-
inhibition kinetics
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
inhibition constants of various organisms
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
-
-
Delta-NB mutant protein
0.02
-
-
Ncut-37 mutant protein
0.11
0.22
-
activity in cell extracts of cells grown on different sugar sources
0.21
-
-
Ccut-101 mutant protein
0.27
-
-
Ccut-32 mutant protein
0.42
-
-
K260A mutant protein
1.57
-
Q975F9
pH 7.5, 80C, substrates: UTP + alpha-D-glucose 1-phosphate
2.1
-
-
Delta 1-4 mutant protein
2.15
-
-
partially purified Golgi apparatus isozyme
3.1
-
-
Ccut-67 mutant protein
3.7
-
-
mutant H191N, pH 7.8, 25C
3.9
-
-
partially purified enzyme
4.76
-
-
partially purified recombinant enzyme
5.4
-
-
Delta 1-8 mutant protein
7.48
-
Q975F9
pH 7.5, 80C, substrates: diphosphate + UDP-alpha-D-glucose
7.8
-
-
mutant K95A, pH 7.8, 25C
8.95
-
-
partially purified enzyme
12.8
-
-
Ncut-21 mutant protein
15.2
-
-
purified enzyme
15.8
-
-
purified enzyme
16
-
-
purified enzyme
200
-
-
purified enzyme
240
-
-
mutant L281D, pH 7.8, 25C
251
-
-
pyrophosphorolysis
340
-
-
UDP-glucose synthesis
385
-
-
UDP-glucose synthesis
449
-
-
UDP-glucose synthesis
495
-
-
purified enzyme
510
-
-
pyrophosphorolysis
591
-
-
Y192A mutant protein
715
-
-
pyrophosphorolysis
752
-
-
K183A mutant protein
764
-
-
K405A mutant protein
853
-
-
K332A mutant protein
899
-
-
purified enzyme
1074
-
-
wild-type protein
1099
-
-
purified enzyme
1200
-
-
purified enzyme
1477
-
-
wild-type, pH 7.8, 25C
1547
-
-
Ccut-8 mutant protein
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
activity in different tissues
additional information
-
-
activity of several mutant strains in vivo
additional information
-
-
Vmax isoenzyme RmlA 37.05, 30C, pH 7.8; Vmax isoenzyme UgpG 1.28, 30C, pH 7.8
additional information
-
-
2-3 fold higher activity in transgenic tibialis anterior, extensor digitorum longus and gastrocnemius muscles than in wild type. Very little increase in activity in transgenic soleus muscle. Transgenes PPL-1 and PPL-2
additional information
-
-
the UGPase protein content and enzyme activity in the Pi-deficient mutant is about twice as high as in wild type and Pi-excess mutants, regardless of the light/dark conditions
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
-
-
activity of UDPGP is significantly up-regulated in muscle tissues from RN- mutants
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
7.5
-
broad
6
7.5
D3HTY9, -
forward reaction
6.5
8.5
-
broad optimum in both reaction directions
7
10.5
-
broad
7
9
-
pyrophosphorolysis
7
9.5
-
broad
7.3
8.6
-
broad
7.5
7.6
-
pyrophosphorolysis
7.5
-
-
assay at
7.5
-
Q975F9
assay at
7.5
-
Q9XUS5
assay at
7.5
-
B8JMZ1
assay at
7.5
-
A5XCL5
assay at
7.5
-
Q16851
assay at
7.5
-
C7GP37
assay at
7.5
-
Q8GQP8, -
-
7.6
9.2
-
broad
7.6
-
-
assay at
7.6
-
Q43772
assay at
7.8
-
-
assay at
8
8.6
-
Golgi membrane and cytosolic isozyme
8
9
-
UDP-glucose synthesis
8
9
-
UDP-glucose synthesis
8
9
-
bovine mammary gland, human erythrocytes
8
-
-
assay at
8.5
-
-
-
additional information
-
-
-
additional information
-
-
active over a wide range
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
isozymes with different pH-optima
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
10
-
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
-
reverse reaction, inactive above pH 10.0 and below pH 5.0, profile overview
7
9
-
about 75% of maximal activity at pH 7.0 and maximal activity at pH 9.0
7.2
9.8
-
about half-maximal activity at pH 7.2 and about 90% of maximal activity at pH 9.8
additional information
-
-
active over a wide range of pH for both forward and reverse reaction
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
21
-
-
assay at
23
-
-
assay at
25
-
-
assay at
25
-
Q43772
assay at
30
-
-
assay at
30
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
Q9XUS5
assay at
37
-
B8JMZ1
assay at
37
-
A5XCL5
assay at
37
-
Q16851
assay at
37
-
C7GP37
assay at
37
-
Q8GQP8, -
-
38
-
-
assay at
80
-
Q975F9
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
45
-
mutant pHC3007
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.9
-
-
Golgi isozyme
4.2
-
-
cytosolic isozyme
4.6
4.7
-
-
5.4
-
-
IEF-PAGE
5.47
-
-
K183A mutant protein; K332A mutant protein; K405A mutant protein
5.54
-
-
Ncut-21 mutant protein
5.55
-
-
Delta 1-8 mutant protein; Delta-NB mutant protein; wild-type protein; Y192A mutant protein
5.58
-
-
Ccut-101 mutant protein
5.63
-
-
Delta 1-4 mutant protein
5.64
-
Q8PK83
calculated
5.69
-
-
Ccut-67 mutant protein
5.7
-
-
Ncut-37 mutant protein
5.79
-
-
Ccut-32 mutant protein
5.8
-
-
Ccut-8 mutant protein
6.1
-
-
calculated for recombinant protein
6.14
-
-
calculated for recombinant protein
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
hypertrophic and nonhypertrophic
Manually annotated by BRENDA team
-
of hypertrophic and nonhypertrophic cells and chondrocytes
Manually annotated by BRENDA team
-
optimization of pullulan production by evaluation of effects of controlled pH on fermentation time, pullulan production, biomass, and UDPG-pyrophosphorylase activity, overview. The activity of UDPG-pyrophosphorylase reaches a maximum at day 3 and decreases sharply after day 4
Manually annotated by BRENDA team
Aureobasidium pullulans CJ001
-
optimization of pullulan production by evaluation of effects of controlled pH on fermentation time, pullulan production, biomass, and UDPG-pyrophosphorylase activity, overview. The activity of UDPG-pyrophosphorylase reaches a maximum at day 3 and decreases sharply after day 4
-
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
-
-
-
Manually annotated by BRENDA team
-
hypertrophic and nonhypertrophic
Manually annotated by BRENDA team
-
; enzyme activity increases during encystment
Manually annotated by BRENDA team
Acanthamoeba castellanii NEFF
-
; enzyme activity increases during encystment
-
Manually annotated by BRENDA team
A3QQQ3
highest expression of enzyme
Manually annotated by BRENDA team
-
male flower, isoform UGP1 is the predominant transcript
Manually annotated by BRENDA team
Q19TV8
expression throughout fruit development
Manually annotated by BRENDA team
-
low level and activity
Manually annotated by BRENDA team
-
isoform UGP1 is the predominant transcript. Isoform UGP1, but not UGP2 is upregulated by light and short-term sucrose feeding. Isoform UGP2 is transiently upregulated by cold treatment
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
-
-
-
Manually annotated by BRENDA team
-
cytosolic and Golgi apparatus isozymes
Manually annotated by BRENDA team
Acetabularia sp., Beta vulgaris subsp. vulgaris var. altissima, Bombyx mori
-
-
Manually annotated by BRENDA team
-
non-germinated
Manually annotated by BRENDA team
A3QQQ3
high expression during anther development
Manually annotated by BRENDA team
Q9M4X0
preferential expression of gene OsUgp in maturing pollens
Manually annotated by BRENDA team
-
low level and activity
Manually annotated by BRENDA team
-
root xylem, isoform UGP1 is the predominant transcript, no upregulation of isoform UGP2 by cold treatment
Manually annotated by BRENDA team
Q9M4X0
old roots but not in young roots
Manually annotated by BRENDA team
-
developing seeds
Manually annotated by BRENDA team
-
predominantly scutellum
Manually annotated by BRENDA team
-
from normal and galactosemic individuals
Manually annotated by BRENDA team
-
isoform UGP2 is upregulated by cold treatment
Manually annotated by BRENDA team
Acanthamoeba castellanii NEFF
-
-
-
Manually annotated by BRENDA team
additional information
-
tissue distribution
Manually annotated by BRENDA team
additional information
-
most abundant in tissues which display active polysaccharide synthesis; tissue distribution
Manually annotated by BRENDA team
additional information
-
enzyme expression is upregulated in hypertrophic chondrocytes compared to nonhypertrophic chondrocytes, 6fold higher mRNA level
Manually annotated by BRENDA team
additional information
-
apart from root xylem, leaf and male flowers, isoforms UGP1 and UGP2 are expressed in similar amounts. Enzyme activity and protein correlate in all tissues and conditions. UGP isoforms generally have lower expressions than sucrose synthases; enzyme activity and protein correlate in all tissues and conditions. UGP isoforms generally have lower expressions than sucrose synthases
Manually annotated by BRENDA team
additional information
A3QQQ3
both isoforms Ugp1 and Ugp2 are ubiquitously expressed throughout rice development, with Ugp1 at much higher levels than Ugp2
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Acetabularia sp., Beta vulgaris subsp. vulgaris var. altissima, Pisum sativum, Zea mays
-
-
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
-
-
-
Manually annotated by BRENDA team
-
UGP3 is a soluble plastid UDP-glucose pyrophosphorylase converts glucose-1-phosphate to UDP-glucose in the stroma
Manually annotated by BRENDA team
Beta vulgaris subsp. vulgaris var. altissima, Bombyx mori, Bos taurus, Canis lupus familiaris, Capra hircus, Columba sp.
-
predominantly, plant or animal cells
Manually annotated by BRENDA team
Trypanosoma brucei 427
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
31500
-
-
SDS-PAGE
45000
-
-
gel filtration
47000
-
-
gel filtration
51000
-
-
gel filtration
51780
-
-
calculated from nucleotide sequence
53000
-
-
gel filtration
53000
-
-
gel filtration
54000
-
-
gel filtration
59000
-
Q4QDU3
gel filtration
120000
-
-
gel filtration
130000
140000
-
gel filtration, dynamic light scattering
130000
-
-
gel filtration
130000
-
-
gel filtration
200000
-
-
gel filtration
270000
-
-
Golgi isozyme, gel filtration
300000
-
-
-
360000
-
-
cytosolic isozyme, gel filtration
390000
-
-
two, non-interconvertible, forms: the second one is lighter and more labile
400000
-
-
sucrose density gradient centrifugation
423700
-
-
gel filtration, recombinant enzyme
430000
-
-
gel filtration
450000
-
-
sucrose density gradient centrifugation
450000
-
-
-
450000
-
-
mammary gland
480000
-
-
sucrose density gradient centrifugation
480000
-
-
multimers of this 480000 MW species exist, ultracentrifugation studies; sucrose density gradient centrifugation
500000
-
-
sucrose density gradient centrifugation
537000
-
-
non-denaturing PAGE
580000
-
-
sucrose density gradient sedimentation
1600000
-
-
gel filtration
5000000
-
-
approximately
additional information
-
Q43772
mixture of monomers, dimers and higher-order polymers, native PAGE and gel filtration, the monomer is the active form
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 51600, about, embryo, amino acid sequence determination
?
-
x * 57000, about DNA sequence determination
?
-
x * 32000, MALDI-TOF of selenomethionine derivative
?
-
x * 53000, SDS-PAGE
?
D3HTY9, -
x * 54507, sequence calculation
?
Trypanosoma brucei 427
-
x * 54507, sequence calculation
-
dimer
-
inactive enzyme form
homodimer
Q4UVD0
2 * 32000, SDS-PAGE, oligomerization detected after crosslinking
homooctamer
Q16851
8 * 55000, SDS-PAGE, human UGPase forms octamers through end-to-end and side-by-side interactions, structure, overview
homooctamer
C7GP37
8 * 55000, SDS-PAGE, the C-terminal left-handed beta-helices are important for the formation of the yUGPase octamer
homotetramer
-, O25363
the tetramerization of HpUGPase does not seem to be related to allosterism
monomer
-
1 * 54000, SDS-PAGE
monomer
-
1 * 55000, SDS-PAGE
monomer
-
1 * 54000, SDS-PAGE
monomer
-
1 * 53000, SDS-PAGE
monomer
-
1 * 51783, calculated from nucleotide sequence
monomer
Q4QDU3
1 * 54500, calculated and SDS-PAGE
monomer
-
53000, native PAGE and SDS-PAGE, calculated without His-tag: 51600 Da; 53000, native PAGE and SDS-PAGE, calculated without His-tag: 51700 Da
monomer
O05576
monomer and different oligomers, gel filtration, x * 36000, SDS-PAGE, x * 35827.0, MALDI-TOF (calculated: 35938.8)
monomer
Q16851
1 * 79000, mutant enzyme N491P/L492E, SDS-PAGE, depolymerization of hUGPase, like in mutant N491P/L492E, results in monomers and higher enzymatic activity
octamer
-
8 * 53000, SDS-PAGE
octamer
-
8 * 56000, SDS-PAGE
octamer
-
8 * 50000, SDS-PAGE, stacked tetrameric configuration
octamer
-
8 * 60000, SDS-PAGE
octamer
-
crystallization data
octamer
Q9XUS5
-
octamer
B8JMZ1
-
octamer
A5XCL5
-
octamer
-
octamers are formed by contacts between highly conserved amino acids in the C-terminal beta-helix
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
tetramer
-
4 * 51000, SDS-PAGE
tetramer
-
4 * 38000, SDS-PAGE
tetramer
-
4 * 30943, SDS-PAGE
tetramer
-
crystallization data
tetramer
P0AEP3
crystallization data
monomer
-
active enzyme form
additional information
-
SDS-PAGE, 4 polypeptides of different MW
additional information
-
multimeric forms may exist
additional information
Q16851
structure comparison of human and yeast enzyme, overview
additional information
C7GP37
structure comparison of human and yeast enzyme, overview
additional information
-
structure-function relationships analysis, overview
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. The ratio of monomers to dimers is about 5:1 in absence of substrate
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
3 putative N-glycosylation sites, possible role in intracellular targeting of the enzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
uncomplexed enzyme and in presence of UTP and UDP-glucose. Structures show a carboxy-terminal beta-helix domain in a unique orientation. The nucleotide binding loop and the carboxy-terminal domain, including the possible catalytically important K360, move in and out of the active site in a concerted fashion
-
from ammonium sulfate precipitate
-
from ammonium sulfate precipitate
-
in complex with both Mg2+ and UDP-glucose. Residues involved in anchoring the ligand to the active site include the polypeptide chain backbone atoms of Ala20, Gly21, Gly117, Gly180, and Ala214, and the side chains of Glu36, Gln112, Asp143, Glu201, and Lys202. Two magnesium ions are coordinated to the UDP-glucose. An alpha- and a beta-phosphoryl oxygen, three waters, and the side chain of Asp142 ligate the first Mg2+ ion, whereas the second ion is coordinated by an alpha-phosphoryl oxygen and five waters; in presence of both magnesium and UDP-glucose. Residues anchoring the ligand to the acitve site include polypepetide backbone atoms of A20, G21, G117, G180 and A214 and side chain residues of E36, Q112, D143, E201, and K202. Two magnesium ions coordinate to UDP-glucose
-, Q6M6R3
protein is a tetramer with 222 point group symmetry. Each subunit is dominated by an eight-stranded mixed beta-sheet with two additional layers of beta-sheets and ten alpha-helices. Q109 and D137 anchor the uracil ring and the ribose of UDP-glucose to the protein.The beta-phosphoryl group of the product lies close to the epsilon-nitrogen of K202, the carboxylate group of E201 can bridge the 2- and 3-hydroxyl groups of the glucosyl moiety; to 1.9 A resolution. Modeling of UDP-glucose into the active site. The side chains of Gln109 and Asp137, respectively, serve to anchor the uracil ring and the ribose of UDP-glucose to the protein. The beta-phosphoryl group of the product is predicted to lie within hydrogen bonding distance to the eosilon-nitrogen of Lys202 whereas the carboxylate group of Glu201 is predicted to bridge the 2'- and 3'-hydroxyl groups of the glucosyl moiety
P0AEP3
apo- and UDP-glucose/Mg2+-bound enzyme complexes, hanging drop and sitting drop vapor diffusion methods, protein in 20 mM Tris-HCl pH 7.5 and 0.1 M NaCl, is mixed with 0.1 M sodium acetate trihydrate, pH 4.6, 2 M ammonium sulfate and 0.1 M guanidine-HCl for the apo-enzyme crystals, 22C, one week. UDP-Glc/Mg2+-bound holo-UGPase is crystallized in 0.1 M HEPES-Na, pH 7.5, 2% PEG 400 and 1.5 M ammonium sulfate containing 10 mM UDP-Glc and 10 mM MgCl2 at 22C within a month, X-ray diffraction structure determination and analysis at 2.9 A and 2.3 A resolutions, respectively
-, O25363
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, 20C, X-ray diffraction structure determination and analysis at 3.6 A resolution, molecular replacement
Q16851
uncomplexed apo-protein with open conformation and in complex with UDP-glucose and closed conformation. the central catalyitc domain resembles a Rossman fold and contains key residues. The C-terminal domain forms a left-handed parallel beta-helix
-
from ammonium sulfate precipitate
-
from ammonium sulfate precipitate
-
both in solution and crystal, enzyme forms homooctamers. Association of octamers is mediated by left-handed helices in the C-terminal domains forming a toroidal solenoid structure. The catalytic domains do not directly contact each other, consistent with simple Michaelis-Menten kinetics
-
detailed comparison between enzyme and thymidylyltransferases; native and seleno-methionine-derivatized proteins, in complex with glucose 1-phosphate, to 2.65 A resolution. Detailed comparison with thymidylyltransferases
-
in complex with glucose 1-phosphate, data from an osmium derivative and a selenomethiomine derivative
-
purified recombinant enzyme, 17 mg/mL protein is mixed 1:1 with a crystallization buffer of 22% PEG 3350, 0.1 M ammonium sulfate, and 0.1 M Bis-Tris, pH 5.5, X-ray diffraction structure determination and analysis at 1.92 A resolution
D3HTY9, -
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
-
-
4C, 80% loss of activity immediately
4
-
-
4C, t1/2: 2 days
5
-
-
86 days, 4C, 70% loss of activity
5.8
-
-
stable
6
8.5
-
47 h, 25C, 0.1 mg/ml bovine serum albumin, 5% loss of activity. Without bovine serum albumin: 80% or 60% loss of activity within 30 h at pH 6 or pH 6.5, respectively, t1/2: 30 h at pH 7.5 and pH 8.5
6.5
7.5
-
86 days, 4C, stable
7.5
9
-
30 min, stable at 50C, in 0.25 M potassium phosphate buffer
7.8
-
-
rapid inactivation above
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
30 h, stable at pH 8.0 with 0.1 mg/ml bovine serum albumin, without bovine serum albumin: t1/2: 7 h
37
-
-
30 min, stable
40
-
-
15 min, 10% loss of activity
47
-
-
t1/2: 10 min
50
-
-
15 min, about 10% or 25% loss of activity of enzymes from normal or galactosemic individuals, respectively
50
-
-
30 min, stable in 0.25 M potassium phosphate buffer, pH 7.5-9.0
50
-
-
15 min, about 15%, 30% or 25% loss of activity with UDP-glucose, UDP-galactose or UDP-xylose as substrate, respectively
50
-
O05576
10 min treatment: about 15% activity
52
-
-
30 min, 70% loss of activity, 0.25 M potassium phosphate buffer, pH 7.5-9.0
56
-
-
15 min: inactivation; t1/2: 4 min
56
-
-
2.5 min: 80% loss of activity in crude desalted extracts
56
-
-
15 min: about 65%, 75% or 95% loss of activity with UDP-glucose, UDP-galactose or UDP-xylose as substrate, respectively
60
-
-
10 min, inactivation
60
-
-
5 min, inactivation
additional information
-
-
isozymes of different heat stability
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
SH-reagents have no effect on enzyme stability
-
reducing agent required for stability
-
glycerol, 25% v/v stabilizes during purification
-
enzyme requires 2-mercaptoethanol for stability
-
bovine serum albumin stabilizes
-
enzyme becomes labile after affinity chromatography purification, probably due to diaggregation
-
enzyme requires 2-mercaptoethanol for stability
-
stable to acid precipitation
-
no reducing agent required for stability
-
stable to dilution to the order of mg/l
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, crude acetone powder, desiccated storage, 2 years
-
PCMB, DTT, iodoacetate or 2-mercaptoethanol does not affect storage stability
-
-20C, crude extract, 25% v/v glycerol, 3-4 weeks
-
0C, unstable upon storage
-
-70C, 50% glycerol, 2 months, no significant loss of activity
-
4C, Tris-HCl buffer, pH 7.5, several months
-
-20C, 20% glycerol, stable at least 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
immobilized metal ion adsorption chromatography; immobilized metal ion adsorption chromatography
-
metal chelation chromatography
-
533fold, multiple forms
-
from liver
-
partial
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Q9XUS5
from liver
-
recombinant protein; recombinant protein
-, Q6M6R3
-
Q19TV8
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
B8JMZ1
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
A5XCL5
recombinant from plasmid, 22.7fold
-
isozyme from Golgi apparatus, 95fold
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-, O25363
from liver
-
recombinant N-terminally StrepII-tagged enzyme from Escherichia coli BL21(DE3) by affinity chromatography
-
recombinant wild-type enzyme, partially from Escherichia coli JM109
-
recombinnat His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Q16851
immobilized metal ion affinity chromatography
-
native and recombinant wild-type, the latter from Escherichia coli to homogeneity
Q43772
recombinant enzyme from Escherichia coli
-
500fold
-
immobilized metal affinity chromatography
O05576
to homogeneity
-
2500fold to homogeneity
-
from liver; preparative sucrose density gradient centrifugation
-
from liver
-
salivary glands: 1 enzyme form, liver: 2 enzyme forms
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
C7GP37
177fold to near homogeneity
-
243fold to near homogeneity
-
ammonium sulfate precipitation, hydrophobic interaction chromatography, anion-exchange chromatography (DEAE)
-
recombinant His-tagged enzyme in Escherichia coli by nickel affinity chromatography
Q8GQP8, -
recombinant His6-tagged enzyme from Escherichia coli strain by nickel affinity chromatography and gel filtration
D3HTY9, -
ammonium sulfate fractionation, ion-exchange chromatography (DEAE)
Q4UVD0
ammonium sulfate fractionation, ion-exchange chromatography (DEAE)
Q8PK83
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens
P57751, Q9M9P3
His-tagged version expressed in Escherichia coli BL21 (DE3); His-tagged version expressed in Escherichia coli BL21 (DE3)
-
His-tagged version expressed in Escherichia coli C41(DE3)
-
UGP3 is highly coexpressed with SQD1 and SQD2
-
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
Q9XUS5
-
Q19TV8
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
B8JMZ1
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
A5XCL5
galU structural gene, DNA sequence determination and analysis, expression from multicopy plasmid
-
expression in chondrocytes with or without co-transfection of HA synthase gene
-
expression in Escherichia coli
-
gene galU, expressio as His-tagged enzyme in Escherichia coli strain BL21(DE3)
-, O25363
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Q16851
expression of the N-terminally StrepII-tagged enzyme in Escherichia coli BL21(DE3)
-
expression of wild-type and mutants in Escherichia coli JM109
-
expression in Escherichia coli
-
from cDNA libraries, 11 clones, DNA and amino acid sequence determination and analysis
-
gene Ugp, expression in Escherichia coli
Q43772
His-tag version expressed in Escherichia coli BL21 (DE3)
-
His-tagged version expressed in Escherichia coli BL21(DE3)
O05576
gene OsUgp2, DNA and amino acid sequence determination and analysis, promoter sequencing and functional analysis employing deletions and gain-of-function experiments in stable transformants, and expression analysis. The spatio-temporal expression of the gene is mostly codetermined by the types, numbers and positions of cisregulatory elements within the promoter region
Q9M4X0
expression in Escherichia coli
-
DNA sequence determination and analysis, gene disruption and depletion of activity is performed, overexpression from multicopy plasmid in haploid strains, on glucose 40fold increased enzyme activity leads to 2fold increase in the concentration of glycogen and UDP-D-glucose, on galactose a 40fold increased activity leads to several effects, e.g. 3fold reduction of growth rate, 3-5fold increase in UDP-D-glucose, UDP-D-galactose and alpha-D-galactose 1-phosphate concentrations, a higher sensitivity to calcofluor white and an increase in the degree of protein glycosylation
-
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
C7GP37
expressed in Escherichia coli BL21 star
-
from cDNA library, DNA sequence determination and analysis
-
expression in Escherichia coli
-
UGP3 is highly coexpressed with SQD1 and SQD2
-
DNA and amino acid sequence determination and analysis, recombinant overepression in Streptococcus zooepidemicus, expression of His-tagged enzyme in Escherichia coli
Q8GQP8, -
expressed in Lactococcus lactis NZ9000
Q8GQP9, -
expression in Escherichia coli
-
expression in Escherichia coli, wild-type and truncated enzyme form lacking the 170-residues C-terminal domain
Q975F9
expression of His6-tagged enzyme in Escherichia coli strain BL21 (DE3)
D3HTY9, -
expressed in Escherichia coli BL21(DE3)
Q4UVD0
expressed in Escherichia coli BL21(DE3)
Q8PK83
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
phosphate starvation
-
UGP1 expression is up-regulated by sucrose in Arabidopsis leaves
-
UGP1 expression is up-regulated by sucrose in Arabidopsis leaves
Arabidopsis thaliana Col-0
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D130A
-, O25363
site-directed mutagenesis the mutant shows highly reduced activity compatred to the wild-type enzyme
R15A
-, O25363
site-directed mutagenesis the mutant shows highly reduced activity compatred to the wild-type enzyme
C123S
-
site-directed mutagenesis, active enzyme, 7fold increase in Km for magnesium diphosphate, 2fold increased Ki for MgUTP2-, no longer sensitive to SH-reagents, e.g. iodoacetamide
E412D
Q16851
site-directed mutagenesis, the mutation does not change the oligomeric state, the mutant shows 176% catalytic activity compared to the wild-type enzyme
E412K
Q16851
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
E412Q
Q16851
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
H266R
-
site-directed mutagenesis, mutant enzyme is active and similar to the wild-type, 4fold decrease in Km and Ki for MgUTP
H446S
-
site-directed mutagenesis, the mutant shows only slight dissociation and slightly reduced activity in forward and reverse reactionsactivity
H497A
-
site-directed mutagenesis, the mutant shows dissociation of subunits, and highly reduced activity in forward and reverse reactions; site-directed mutagenesis, the mutant shows only slight dissociation and retains full activity in the reverse eaction, but shows reduced reaction in the forward reaction
I466T
-
site-directed mutagenesis, the mutant shows dissociation of subunits, a tetramer appears in addition to di- and monomers, and highly reduced activity in forward and reverse reactions
I468K
-
site-directed mutagenesis, the mutant shows dissociation of subunits, a tetramer appears in addition to di- and monomers, the mutant shows reduced activity in the reverse reaction
I487D
-
site-directed mutagenesis, the mutant shows dissociation of subunits, and highly reduced activity in forward and reverse reactions
K4110S
Q16851
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
N391P/L492E
-
site-directed mutagenesis, inactive mutant showing dissociation into di- and monomers
N491P
-
site-directed mutagenesis, the mutant shows reduced activity in the reverse reaction
N491P/L492E
Q16851
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
P414G/T415P
Q16851
site-directed mutagenesis, the mutant shows activity similar to that of the wild-type hUGPase, the mutation does not change the oligomeric state
R389H
-
site-directed mutagenesis, mutant enzyme is active and similar to the wild-type
R391K
-
site-directed mutagenesis, no activity, no correct folding
R422Q
-
site-directed mutagenesis, mutant enzyme is active and similar to the wild-type
R445H
-
site-directed mutagenesis, mutant enzyme is active and similar to the wild-type
S309N/S311R
Q16851
site-directed mutagenesis, mutation in sequence analogy to the Saccharomyces cerevisiae enzyme, the mutant shows 84% of wild-type activity
T406K/M407L
Q16851
site-directed mutagenesis, the mutant shows activity similar to that of the wild-type hUGPase, the mutation does not change the oligomeric state
T448K
-
site-directed mutagenesis, the mutant shows dissociation of subunits, a tetramer appears in addition to di- and monomers, and highly reduced activity in forward and reverse reactions
V416N
Q16851
site-directed mutagenesis, the mutant shows activity similar to that of the wild-type hUGPase, the mutation does not change the oligomeric state
W218S
-
site-directed mutagenesis, mutant enzyme is active and similar to the wild-type, increase in Km
W333S
-
site-directed mutagenesis, no activity, no correct folding
C99S
Q43772
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
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
H191L
-
no residual activity
H191N
-
0.3% of wild-type activity
K380D
-
no residual activity
K95A
-
0.5% of wild-type activity
additional information
-
enzyme gene disruption mutant reduces the survival of Aeromonas hydrophila in serum to less than 1%, decreases the ability of strains to adhere and reduces by 1.5 or 2 log units the virulence of Aeromonas serotype O34 strains in a septicaemia model. The mutant shows two types of lipopolysaccharide structures. The first one corresponds to a rough strain having the complete core, but lacking the terminal galactose residue from the LPS-core and 4-amino-4-deoxyarabinose residues from phosphate groups in lipid A. The second one corresponds to a deeply truncated structure with the LPS-core restricted to one 3-deoxy-D-manno-oct-2-ulosonic acid and three L-glycero-D-manno-heptose residues
additional information
-
construction of transgenic plants, with increased or deleted expression of enzyme, study of sucrose effects on the enzyme and gene Ugp, respectively
additional information
-
UGP2 is unable to replace UGP1 in UGP1 knockout lines
additional information
Arabidopsis thaliana Col-0
-
UGP2 is unable to replace UGP1 in UGP1 knockout lines
-
L492E
-
site-directed mutagenesis, the mutant shows only slight dissociation and retains activity
additional information
-
truncation mutant DELTA 490-497 is almost inactive due to dissociation into di- and monomers
K405A
-
possibly involved in subunit interaction
additional information
Q43772
amino acid exchanges in hydrophobic domain
L281D
-
16.3% of wild-type activity
additional information
-
overexpression of sucrose synthase and of UDP-glucose pyrophosphorylase. Single transgenic plants show significant increases in the height growth. Double-transgene plants demonstrate an additive effect and are even taller than single-transgene parents. Double-transgene plants may show increases in soluble sugar content. Both enzymes may be markers for sink strength
D462H
A3QQQ3
natural mutation of isoform Ugp1, D462 in rice variety B5 is replaced by H462 in rice variety TN1
additional information
A3QQQ3
isoform Ugp1 silencing by RNAi results in male sterility of plants. Pollen mother cells of silenced plants appear normal before meiosis, but during meiosis, normal callose deposition is disrupted and the degeneration of the tapetum and middle layer is inhibited
additional information
Q9M4X0
generation of gain-of-function promoter-GUS fusion constructs, overview
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
UDP glucose diphosphorylase is an allergen in natural rubber latex and able to cause latex-fruit allergy syndroms. It may act as a potential pan-allergen in vegetable foods
synthesis
-
easy available enzyme can be used for synthesis of nucleotide sugars in enzymic glycoconjugate synthesis
agriculture
-
overexpression of sucrose synthase and of UDP-glucose pyrophosphorylase. Single transgenic plants show significant increases in the height growth. Double-transgene plants demonstrate an additive effect and are even taller than single-transgene parents. Double-transgene plants may show increases in soluble sugar content. Both enzymes may be markers for sink strength