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Information on EC 2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P32861
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2.7.7.9 UTP-glucose-1-phosphate uridylyltransferaseSpecify your search results
Word Map
- 2.7.7.9
- phosphoglucomutase
- polysaccharide
- glycogen
- galactose
- udp-galactose
- adp-glucose
- exopolysaccharide
- dictyostelium
- udp-sugars
- udp-n-acetylglucosamine
-
leloir
- galactose-1-phosphate
-
udp-glucuronic
- galactokinase
-
aureobasidium
-
pyrophosphorolysis
-
sucrose-phosphate
- gellan
- xylinum
- agriculture
- synthesis
- medicine
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
udp-glucose pyrophosphorylase, ugpase, udpg-pyrophosphorylase, udpgp, udp-glc pyrophosphorylase, udpglucose pyrophosphorylase, glucose-1-phosphate uridylyltransferase, udpg pyrophosphorylase, utp-glucose-1-phosphate uridylyltransferase, uridine diphosphoglucose pyrophosphorylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glucose 1-phosphate uridylyltransferase
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glucose-1-phosphate uridylyltransferase
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UDP glucose pyrophosphorylase
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UDP-glucose pyrophosphorylase
UDPG phosphorylase
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UDPG pyrophosphorylase
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UDPglucose pyrophosphorylase
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UGPase
uridine 5'-diphosphoglucose pyrophosphorylase
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uridine diphosphate-D-glucose pyrophosphorylase
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uridine diphosphoglucose pyrophosphorylase
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uridine-diphosphate glucose pyrophosphorylase
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uridylyltransferase, glucose 1-phosphate
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UDP-glucose pyrophosphorylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
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PATHWAY SOURCE
PATHWAYS
KEGG
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-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
UTP:alpha-D-glucose-1-phosphate uridylyltransferase
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CAS REGISTRY NUMBER
COMMENTARY
9026-22-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
farnesyl triphosphate + UDP-glucose
farnesyl-tetraphosphouridine + alpha-D-glucose + diphosphate
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-
-
-
?
geranyl triphosphate + UDP-glucose
geranyl-tetraphosphouridine + alpha-D-glucose + diphosphate
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-
-
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?
isopentenyl triphosphate + UDP-glucose
isopentenyl-tetraphosphouridine + alpha-D-glucose + diphosphate
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-
-
-
?
methylenebisphosphonate + UDP-glucose
uridine 5'-(beta,gamma-methylenetriphosphate) + alpha-D-glucose + diphosphate
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-
-
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?
monothiodiphosphate + UDP-glucose
UTPbeta,gammaS + alpha-D-glucose 1-phosphate
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poor substrate, 4.8% of Vmax with diphosphate
UTPbeta,gammaS is chemically unstable and undergoes hydrolysis to UDPbetaS and phosphate, which renders the otherwise reversible reaction irreversible, t1/2 at 25°C: 0.5 min
ir
UDP-glucose + adenosine 5'-tetraphosphate
D-glucose-1-phosphate + adenosyl-5'-pentaphospho-5'-uridine
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-
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?
UDP-glucose + ATP
D-glucose-1-phosphate + adenosyl-5'-tetraphospho-5'-uridine
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?
UDP-glucose + CTP
D-glucose-1-phosphate + cytidinyl-5'-tetraphospho-5'-uridine
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-
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?
UDP-glucose + GTP
D-glucose-1-phosphate + guanosyl-5'-tetraphospho-5'-uridine
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-
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?
UDP-glucose + guanosine 5'-tetraphosphate
D-glucose-1-phosphate + guanosyl-5'-pentaphospho-5'-uridine
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-
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?
UDP-glucose + tetrapolyphosphate
uridine-5'-pentaphosphate + D-glucose-1-phosphate
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?
UDP-glucose + tripolyphosphate
uridine-5'-tetraphosphate + D-glucose-1-phosphate
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?
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
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-
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r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
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r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
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r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
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r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
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r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
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r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
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r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
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r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
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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
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enzyme is essential for cell viability
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?
additional information
?
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UDP-galactose is not a UMP-donor and ADP not a UMP-acceptor
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?
additional information
?
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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
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
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r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
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-
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r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
activation of glucosyl residues for glycogen synthesis, participates in synthesis of numerous compounds including cell wall polymers in higher plants and microorganisms, starch, trehalose, glycosides, glycolipids, heparin, microbial antigens, lactose, glucuronides, and rhamnose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
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enzyme is essential for cell viability
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.83
alpha-D-glucose 1-phosphate
pH 7.5, 37°C, recombinant enzyme
additional information
additional information
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kinetic parameters of various organisms, pH 8.0, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
inhibition constants of various organisms
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
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most abundant in tissues which display active polysaccharide synthesis
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
a knockdown mutant of Ugp1 exhibits an impaired mobilization of glycogen and trehalose as well as a reduction in oxidative stress resistance and long-term cell survival during stationary phase. The modulation of Ugp1 level readjusts glycogen and trehalose accumulation in the protein kinase A-related gene mutants. The protein kinase A-dependent phenotypes of oxidative stress resistance and long-term cell survival are also alleviated via adjustment of Ugp1 level
additional information
structure comparison of human and yeast enzyme, overview
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55000
8 * 55000, SDS-PAGE, the C-terminal left-handed beta-helices are important for the formation of the yUGPase octamer
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homooctamer
8 * 55000, SDS-PAGE, the C-terminal left-handed beta-helices are important for the formation of the yUGPase octamer
additional information
structure comparison of human and yeast enzyme, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
inc finger transcription factors Msn2 and Msn4 bind to three stress response elements in the UGP1 promoter in a protein kinase A-dependent manner. Several stresses induce UGP1 transcription, suggesting that the regulation of UGP1 mediated by Msn2/4 is involved in general stress response. The phosphate response pathway also controls Msn2/4-dependent regulation of UGP1
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kalckar, H.M.
The role of phosphoglycosyl compounds in the biosynthesis of nucleosides and nucleotides
Biochim. Biophys. Acta
12
250-264
1953
Saccharomyces cerevisiae, Saccharomyces fragilis
Turnquist, R.L.; Hansen, R.G.
Uridine diphosphoryl glucose pyrophosphorylase
The Enzymes, 3rd. Ed. (Boyer, P. D. , ed. )
8
51-71
1973
Acetabularia sp., Beta vulgaris subsp. vulgaris, Bombyx mori, Bos taurus, Saccharomyces cerevisiae, Canis lupus familiaris, Capra hircus, Gallus gallus, Columba sp., Oryctolagus cuniculus, Dictyostelium discoideum, Escherichia coli, Ovis aries, Homo sapiens, Pisum sativum, Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium, Zea mays
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Daran, J.M.; Dallies, N.; Thines-Sempoux, D.; Paquet, V.; Francois, J.
Genetic and biochemical characterization of the UGP1 gene encoding the UDP-glucose pyrophosphorylase from Saccharomyces cerevisiae
Eur. J. Biochem.
233
520-530
1995
Saccharomyces cerevisiae
Lightcap, E.S.; Frey, P.A.
m-Monothiopyrophosphate as a substrate for inorganic pyrophosphatase and UDP-glucose pyrophosphorylase
Arch. Biochem. Biophys.
335
183-190
1996
Saccharomyces cerevisiae
Guranowski, A.; de Diego, A.; Sillero, A.; Gunther Sillero, M.A.
Uridine 5'-polyphosphates (p4U and p5U) and uridine(5')polyphospho(5')nucleosides (Up(n)Ns) can be synthesized by UTP:glucose-1-phosphate uridylyltransferase from Saccharomyces cerevisiae
FEBS Lett.
561
83-88
2004
Saccharomyces cerevisiae
Roeben, A.; Plitzko, J.M.; Koerner, R.; Boettcher, U.M.; Siegers, K.; Hayer-Hartl, M.; Bracher, A.
Structural basis for subunit assembly in UDP-glucose pyrophosphorylase from Saccharomyces cerevisiae
J. Mol. Biol.
364
551-560
2006
Saccharomyces cerevisiae
Yu, Q.; Zheng, X.
The crystal structure of human UDP-glucose pyrophosphorylase reveals a latch effect that influences enzymatic activity
Biochem. J.
442
283-291
2012
Drosophila melanogaster (A5XCL5), Danio rerio (B8JMZ1), Saccharomyces cerevisiae (C7GP37), Homo sapiens (Q16851), Homo sapiens, Caenorhabditis elegans (Q9XUS5)
Guenther Sillero, M.A.; de Diego, A.; Sillero, A.
Methylenebisphosphonate and triphosphate derivatives of the mevalonate pathway are substrates of yeast UTP:glucose-1-phosphate uridylyltransferase
Biochimie
94
1871-1875
2012
Saccharomyces cerevisiae
Yi, D.; Huh, W.
UDP-glucose pyrophosphorylase Ugp1 is involved in oxidative stress response and long-term survival during stationary phase in Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
467
657-6632
2015
Saccharomyces cerevisiae (P32861)
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