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Information on EC 2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase and Organism(s) Escherichia coli and UniProt Accession P0AEP3
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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
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udp-glucuronic
- galactokinase
-
aureobasidium
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pyrophosphorolysis
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sucrose-phosphate
- gellan
- xylinum
- agriculture
- synthesis
- medicine
The taxonomic range for the selected organisms is: Escherichia coli
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
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UDPG phosphorylase
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UDPG pyrophosphorylase
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UDPglucose pyrophosphorylase
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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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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
UDP-D-glucose + diphosphate
UTP + alpha-D-glucose 1-phosphate
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-
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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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central reaction in galactose and trehalose metabolism
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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
UDP-D-glucose + diphosphate
UTP + alpha-D-glucose 1-phosphate
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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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central reaction in galactose and trehalose metabolism
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-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
INHIBITOR
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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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
7.8
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
galU structural gene, DNA sequence determination and analysis, expression from multicopy plasmid
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Weissborn, A.C.; Liu, Q.; Rumley, M.K.; Kennedy, E.P.
UTP: alpha-D-glucose-1-phosphate uridylyltransferase of Escherichia coli: isolation and DNA sequence of the galU gene and purification of the enzyme
J. Bacteriol.
176
2611-2618
1994
Escherichia coli
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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Thoden, J.B.; Holden, H.M.
The molecular architecture of glucose-1-phosphate uridylyltransferase
Protein Sci.
16
432-440
2007
Escherichia coli (P0AEP3), Escherichia coli
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