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Information on EC 2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase and Organism(s) Hordeum vulgare and UniProt Accession Q43772
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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: Hordeum vulgare
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
-
-
-
-
glucose-1-phosphate uridylyltransferase
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-
-
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UDP glucose pyrophosphorylase
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-
-
-
UDP-glucose pyrophosphorylase
UDPG phosphorylase
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-
-
-
UDPG pyrophosphorylase
-
-
-
-
UDPglucose pyrophosphorylase
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-
-
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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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-
-
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uridine diphosphoglucose pyrophosphorylase
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-
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uridine-diphosphate glucose pyrophosphorylase
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-
-
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uridylyltransferase, glucose 1-phosphate
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-
-
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UDP-glucose pyrophosphorylase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -
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
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
-
low activity
-
-
r
additional information
?
-
-
the enzyme catalyses a freely reversible reaction and is specific for alpha-D-glucose 1-phosphate
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
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-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
key enzyme in biosynthesis of sucrose, cellulose, and other saccharides
-
r
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
key enzyme in biosynthesis of sucrose, cellulose, and other saccharides
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
alpha-D-galactose 1-phosphate
-
pH 7.5, temperature not specified in the publication
0.033
alpha-D-glucose 1-phosphate
-
pH 7.5, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
-
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.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.47
5.55
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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_HORVU
473
0
51644
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
mixture of monomers, dimers and higher-order polymers, native PAGE and gel filtration, the monomer is the active form
additional information
-
mixture of monomers, dimers and higher-order polymers, native PAGE and gel filtration, the monomer is the active form
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
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
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
3 putative N-glycosylation sites, possible role in intracellular targeting of the enzyme
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C99S
site-directed mutagenesis, half Vmax of wild-type, 12fold higher Km for diphosphate, altered diphosphate binding
Ccut-101
101 amino acid residues deleted (exons 16-19, and 1 amino acid residue of exon 15)
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)
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native and recombinant wild-type, the latter from Escherichia coli to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
from cDNA libraries, 11 clones, DNA and amino acid sequence determination and analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eimert, K.; Villand, P.; Kilian, A.; Kleczkowski, L.A.
Cloning and characterization of several cDNAs for UDP-glucose pyrophosphorylase from barley (Hordeum vulgare) tissues
Gene
170
227-232
1996
Hordeum vulgare (Q43772), Hordeum vulgare
Martz, F.; Wilczynska, M.; Kleczkowski, L.A.
Oligomerization status, with the monomer as active species, defines catalytic efficiency of UDP-glucose pyrophosphorylase
Biochem. J.
367
295-300
2002
Hordeum vulgare (Q43772), Hordeum vulgare
Kleczkowski, L.A.; Martz, F.; Wilczynska, M.
Factors affecting oligomerization status of UDP-glucose pyrophosphorylase
Phytochemistry
66
2815-2821
2005
Hordeum vulgare (Q43772), Hordeum vulgare
Meng, M.; Fitzek, E.; Gajowniczek, A.; Wilczynska, M.; Kleczkowski, L.A.
Domain-specific determinants of catalysis/substrate binding and the oligomerization status of barley UDP-glucose pyrophosphorylase
Biochim. Biophys. Acta
1794
1734-1742
2009
Hordeum vulgare (Q43772), Hordeum vulgare
Decker, D.; Meng, M.; Gornicka, A.; Hofer, A.; Wilczynska, M.; Kleczkowski, L.A.
Substrate kinetics and substrate effects on the quaternary structure of barley UDP-glucose pyrophosphorylase
Phytochemistry
79
39-45
2012
Hordeum vulgare
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