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Information on EC 2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase and Organism(s) Homo sapiens and UniProt Accession Q16851
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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
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sucrose-phosphate
- gellan
- xylinum
- agriculture
- synthesis
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
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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-
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UDPG pyrophosphorylase
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UDPglucose pyrophosphorylase
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uridine 5'-diphosphoglucose pyrophosphorylase
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-
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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
Trp333 and Arg391 are essential for activity, while His266, Arg389, Arg422, Arg 445, and Trp218 are not
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
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-
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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
diphosphate + GDP-glucose
GTP + alpha-D-glucose 1-phosphate
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calf and human liver, poor substrate
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r
diphosphate + UDP-mannose
UTP + D-mannose 1-phosphate
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calf and human liver, poor substrate
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r
diphosphate + CDP-glucose
CTP + alpha-D-glucose 1-phosphate
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calf and human liver, poor substrate
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r
diphosphate + CDP-glucose
CTP + alpha-D-glucose 1-phosphate
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very low activity, wild-type and mutant W218
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r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
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poor substrate
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
-
poor substrate
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
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poor substrate
-
r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
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calf and human liver
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r
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
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very low activity, wild-type and mutant W218
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r
diphosphate + UDP-xylose
UTP + D-xylose 1-phosphate
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poor substrate
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-
r
diphosphate + UDP-xylose
UTP + D-xylose 1-phosphate
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calf and human liver
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-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
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reverse reaction: calf and human liver
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r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
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1-12% of the activity with 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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specific for alpha-D-glucose 1-phosphate
specific for UDP-glucose
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
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highly specific for UTP
specific for UDP-glucose
r
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
-
-
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
UDP
UGPase activity is not significantly decreases in A-549 cells treated with 0.0001-0.003 mM UDP. Activity is significantly decreased at 0.005 mM and 0.1 mM UDP treatments. The inhibition of UGPase activity in A549 cells is 28fold higher at 0.1 mM UDP treatment in comparison to 0.005 mM treatment
iodoacetamide
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wild-type: loss of 56% activity after 30 min at 0.1 mM, mutant C123S is not affected
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic parameters of various organisms, pH 8.0, overview
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0.198
alpha-D-glucose 1-phosphate
pH 7.5, 37°C, recombinant mutant N491P/L492E
0.202
alpha-D-glucose 1-phosphate
pH 7.5, 37°C, recombinant mutant P414G/T415P
0.219
alpha-D-glucose 1-phosphate
pH 7.5, 37°C, recombinant mutant T406K/M407L
0.235
alpha-D-glucose 1-phosphate
pH 7.5, 37°C, recombinant mutant S309N/S311R
0.68 - 1
alpha-D-glucose 1-phosphate
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recombinant wild-type enzyme, pH 8.0, 25°C
TURNOVER NUMBER [1/s]
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
-
most abundant in tissues which display active polysaccharide synthesis
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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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
additional information
additional information
structure comparison of human and yeast enzyme, overview. Depolymerization of hUGPase, like in mutant N491P/L492E, results in monomers and higher enzymatic activity
additional information
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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
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hUGPs are active in the octameric state and do not dissociate during the enzymatic cycle, structure-function relationships analysis, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). UGPA_HUMAN
508
0
56940
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55000
8 * 55000, SDS-PAGE, human UGPase forms octamers through end-to-end and side-by-side interactions, structure, overview
79000
1 * 79000, mutant enzyme N491P/L492E, SDS-PAGE, depolymerization of hUGPase, like in mutant N491P/L492E, results in monomers and higher enzymatic activity
450000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homooctamer
8 * 55000, SDS-PAGE, human UGPase forms octamers through end-to-end and side-by-side interactions, structure, overview
monomer
1 * 79000, mutant enzyme N491P/L492E, SDS-PAGE, depolymerization of hUGPase, like in mutant N491P/L492E, results in monomers and higher enzymatic activity
octamer
additional information
octamer
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octamers are formed by contacts between highly conserved amino acids in the C-terminal beta-helix
additional information
structure comparison of human and yeast enzyme, overview
additional information
-
structure comparison of human and yeast enzyme, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in the D4 octameric structure of the hUGP1-UDP-Glc complex, all subunits have the same overall conformation. The transition of the UGP octamer between the apo- and the product-bound forms is in agreement with the Monod-Wyman-Changeux symmetry model. oligomerzation facilitates an intermolecular stabilization of the sugar moiety in the active site (interlock mechanism), enhances protein stability, enables mild positive cooperativity observed for the octameric wild-type UGP1 towards diphosphate in the reverse reaction, and may allow regulation of the UGP octamer by modification of a single subunit
purified recombinant enzyme, hanging drop vapour diffusion method, mixing of 0.002 ml of 10 mg/ml protein in 20 mM Tris/HCl, pH 8.0, and 200 mM NaCl, with 0.001 ml of reservoir solution containing 100 mM HEPES, pH 6.5, 5 mM MgSO4, 15% w/v PEG 3350 and 20% v/v glycerol, 20°C, X-ray diffraction structure determination and analysis at 3.6 A resolution, molecular replacement
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E412D
site-directed mutagenesis, the mutation does not change the oligomeric state, the mutant shows 176% catalytic activity compared to the wild-type enzyme
E412K
site-directed mutagenesis, the mutant has a longer side chain with a reverse in charge showed obvious inhibitory effects which results in 78% reduced activity compared to the wild-type hUGPase activity
E412Q
site-directed mutagenesis, the mutation changes the charge property, but not the length of side chain and shows only a marginal increase in activity of 19% when compared with the wild-type protein
K4110S
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
N491P/L492E
site-directed mutagenesis, mutant N491P/L492E is constructed to depolymerize hUGPase octamers, the mutation in the C-terminal left-handed beta-helix changes the oligomerization state the mutant enzyme, that becomes monomeric, it shows about the double activity of the wild-type enzyme
P414G/T415P
site-directed mutagenesis, the mutant shows activity similar to that of the wild-type hUGPase, the mutation does not change the oligomeric state
S309N/S311R
site-directed mutagenesis, mutation in sequence analogy to the Saccharomyces cerevisiae enzyme, the mutant shows 84% of wild-type activity
T406K/M407L
site-directed mutagenesis, the mutant shows activity similar to that of the wild-type hUGPase, the mutation does not change the oligomeric state
V416N
site-directed mutagenesis, the mutant shows activity similar to that of the wild-type hUGPase, the mutation does not change the oligomeric state
C123S
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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
H266R
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site-directed mutagenesis, mutant enzyme is active and similar to the wild-type, 4fold decrease in Km and Ki for MgUTP
H446S
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site-directed mutagenesis, the mutant shows only slight dissociation and slightly reduced activity in forward and reverse reactionsactivity
H497A
I466T
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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
L492E
-
site-directed mutagenesis, the mutant shows only slight dissociation and retains activity
N391P/L492E
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site-directed mutagenesis, inactive mutant showing dissociation into di- and monomers
N491P
-
site-directed mutagenesis, the mutant shows reduced activity in the reverse reaction
R389H
-
site-directed mutagenesis, mutant enzyme is active and similar to the wild-type
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
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
W218S
-
site-directed mutagenesis, mutant enzyme is active and similar to the wild-type, increase in Km
additional information
-
truncation mutant DELTA 490-497 is almost inactive due to dissociation into di- and monomers
H497A
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site-directed mutagenesis, the mutant shows dissociation of subunits, and highly reduced activity in forward and reverse reactions
H497A
-
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
56
50
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15 min, about 15%, 30% or 25% loss of activity with UDP-glucose, UDP-galactose or UDP-xylose as substrate, respectively
50
-
15 min, about 10% or 25% loss of activity of enzymes from normal or galactosemic individuals, respectively
56
-
15 min: about 65%, 75% or 95% loss of activity with UDP-glucose, UDP-galactose or UDP-xylose as substrate, respectively
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinnat His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant N-terminally StrepII-tagged enzyme from Escherichia coli BL21(DE3) by affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
expression of the N-terminally StrepII-tagged enzyme in Escherichia coli BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chacko, C.M.; McCrone, L.; Nadler, H.L.
Uridine diphosphoglucose pyrophosphorylase and uridine diphosphogalactose pyrophosphorylase in human skin fibroblasts derived from normal and galactosemic individuals
Biochim. Biophys. Acta
268
113-120
1972
Homo sapiens
Turnquist, R.L.; Turnquist, M.M.; Bachmann, R.C.; Hansen, R.G.
Uridine diphosphate glucose pyrophosphorylase: differential heat inactivation and further characterization of human liver enzyme
Biochim. Biophys. Acta
364
59-67
1974
Homo sapiens
Turnquist, R.L.; Gillett, T.A.; Hansen, R.G.
Uridine diphosphate glucose pyrophosphorylase. Crystallization and properties of the enzyme from rabbit liver and species comparisons
J. Biol. Chem.
249
7695-7700
1974
Bos taurus, Oryctolagus cuniculus, Homo sapiens
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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Chang, H.Y.; Peng, H.L.; Chao, Y.C.; Duggleby, R.G.
The importance of conserved residues in human liver UDPglucose pyrophosphorylase
Eur. J. Biochem.
236
723-728
1996
Homo sapiens
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)
Fuehring, J.; Damerow, S.; Fedorov, R.; Schneider, J.; Muenster-Kuehnel, A.K.; Gerardy-Schahn, R.
Octamerization is essential for enzymatic function of human UDP-glucose pyrophosphorylase
Glycobiology
23
426-437
2013
Homo sapiens
Fuehring, J.I.; Cramer, J.T.; Schneider, J.; Baruch, P.; Gerardy-Schahn, R.; Fedorov, R.
A quaternary mechanism enables the complex biological functions of octameric human UDP-glucose pyrophosphorylase, a key enzyme in cell metabolism
Sci. Rep.
5
9618
2015
Homo sapiens (Q16851), Homo sapiens
Sharma, M.; Sharma, S.; Ray, P.; Chakraborti, A.
Targeting Streptococcus pneumoniae UDP-glucose pyrophosphorylase (UGPase) in vitro validation of a putative inhibitor
Drug Target Insights
14
26-33
2020
Streptococcus pneumoniae (A0A0H2ZMV4), Streptococcus pneumoniae, Homo sapiens (Q16851), Homo sapiens
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