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Information on EC 2.4.1.305 - UDP-Glc:alpha-D-GlcNAc-glucosaminyl-diphosphoundecaprenol beta-1,3-glucosyltransferase
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EC Tree
2.4.1.305 UDP-Glc:alpha-D-GlcNAc-glucosaminyl-diphosphoundecaprenol beta-1,3-glucosyltransferaseIUBMB Comments
The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Escherichia coli serotype O56 and serotype O152.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
UDP-Glc:GlcNAc-pyrophosphate-lipid beta-1,3-glucosyltransferase, WfaP, WfgD, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
UDP-Glc:GlcNAc-pyrophosphate-lipid beta-1,3-glucosyltransferase
WfaP
WfgD
UDP-Glc:GlcNAc-pyrophosphate-lipid beta-1,3-glucosyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-glucose:N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol beta-1,3-glucosyltransferase
The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Escherichia coli serotype O56 and serotype O152.
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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-alpha-D-glucose + alpha-D-GlcNAc-diphospho-(CH2)9-CH3
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-(CH2)9-CH3
UDP-alpha-D-glucose + alpha-D-GlcNAc-diphospho-16-phenoxyhexadecanol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-16-phenoxyhexadecanol
UDP-alpha-D-glucose + alpha-D-GlcNAc-diphospho-6-phenoxyhexanol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-6-phenoxyhexanol
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-(CH2)9-CH3
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-(CH2)9-CH3
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-11-phenoxyundecanol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-11-phenoxyundecanol
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-16-phenoxyhexadecanol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-16-phenoxyhexadecanol
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-6-phenoxyhexanol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-6-phenoxyhexanol
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?
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
UDP-alpha-D-glucose + alpha-D-GlcNAc-diphospho-(CH2)9-CH3
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-(CH2)9-CH3
150% of the activity compared to N-acetyl-alpha-D-glucosaminyl-diphospho-11-phenoxyundecaprenol as acceptor substrate
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?
UDP-alpha-D-glucose + alpha-D-GlcNAc-diphospho-(CH2)9-CH3
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-(CH2)9-CH3
150% of the activity compared to N-acetyl-alpha-D-glucosaminyl-diphospho-11-phenoxyundecaprenol as acceptor substrate
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?
UDP-alpha-D-glucose + alpha-D-GlcNAc-diphospho-16-phenoxyhexadecanol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-16-phenoxyhexadecanol
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?
UDP-alpha-D-glucose + alpha-D-GlcNAc-diphospho-16-phenoxyhexadecanol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-16-phenoxyhexadecanol
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?
UDP-alpha-D-glucose + alpha-D-GlcNAc-diphospho-6-phenoxyhexanol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-6-phenoxyhexanol
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-
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?
UDP-alpha-D-glucose + alpha-D-GlcNAc-diphospho-6-phenoxyhexanol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-6-phenoxyhexanol
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-
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?
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-(CH2)9-CH3
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-(CH2)9-CH3
32% of the activity compared to N-acetyl-alpha-D-glucosaminyl-diphospho-11-phenoxyundecaprenol as acceptor substrate
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-
?
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-(CH2)9-CH3
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-(CH2)9-CH3
32% of the activity compared to N-acetyl-alpha-D-glucosaminyl-diphospho-11-phenoxyundecaprenol as acceptor substrate
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?
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-11-phenoxyundecanol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-11-phenoxyundecanol
the enzyme requires the diphosphate-sugar linkage in the acceptor substrate for full activity. Substrates lacking diphosphate linked to GlcNAc are inactive. An acceptor analog containing a single phosphate group (D-GlcNAc-alpha-diphospho-11-phenoxyundecanol) shows 11% activity. The phenyl group is not required for activity. The length of the aliphatic chain of acceptor substrates also contributes to the activity. The synthetic acceptor N-acetyl-alpha-D-glucosaminyl-diphospho-11-phenoxyundecaprenol is an analog of the natural undecaprenol-pyrophosphate-sugar acceptor substrate. No activity with CMP-sialic acid, UDP-GlcNAc, UDP-GalNAc, or GDP-Man as donor substrate. UDP-Gal shows 0.2% of the activity compared to UDP-D-glucose
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?
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-11-phenoxyundecanol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-11-phenoxyundecanol
the enzyme requires the diphosphate-sugar linkage in the acceptor substrate for full activity. Substrates lacking diphosphate linked to GlcNAc are inactive. An acceptor analog containing a single phosphate group (D-GlcNAc-alpha-P-(CH2)11-O-Ph) shows 1% activity. The phenyl group is not required for activity. The length of the aliphatic chain of acceptor substrates also contributes to the activity. The synthetic acceptor N-acetyl-alpha-D-glucosaminyl-diphospho-11-phenoxyundecaprenol is an analog of the natural undecaprenol-diphosphate-sugar acceptor substrate. No activity with CMP-sialic acid, UDP-GlcNAc, UDP-GalNAc, or GDP-Man as donor substrate. UDP-Gal shows 0.6% of the activity compared to UDP-D-glucose
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?
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-11-phenoxyundecanol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-11-phenoxyundecanol
the enzyme requires the diphosphate-sugar linkage in the acceptor substrate for full activity. Substrates lacking diphosphate linked to GlcNAc are inactive. An acceptor analog containing a single phosphate group (D-GlcNAc-alpha-P-(CH2)11-O-Ph) shows 1% activity. The phenyl group is not required for activity. The length of the aliphatic chain of acceptor substrates also contributes to the activity. The synthetic acceptor N-acetyl-alpha-D-glucosaminyl-diphospho-11-phenoxyundecaprenol is an analog of the natural undecaprenol-diphosphate-sugar acceptor substrate. No activity with CMP-sialic acid, UDP-GlcNAc, UDP-GalNAc, or GDP-Man as donor substrate. UDP-Gal shows 0.6% of the activity compared to UDP-D-glucose
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?
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-16-phenoxyhexadecanol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-16-phenoxyhexadecanol
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?
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-16-phenoxyhexadecanol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-16-phenoxyhexadecanol
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?
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
the enzyme catalyzes the formation of the Glc-(1->3)-GlcNAc linkage in the repeating units of the O-antigen oligosaccharide of Escherichia coli serotype O152
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?
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
the enzyme catalyzes the formation of the Glc-1-3-GlcNAc linkage in the repeating units of the O-antigen oligosaccharide Of Escherichia coli serotype O56
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?
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
the enzyme catalyzes the formation of the Glc-(1->3)-GlcNAc linkage in the repeating units of the O-antigen oligosaccharide of Escherichia coli serotype O152
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-
?
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
the enzyme catalyzes the formation of the Glc-1-3-GlcNAc linkage in the repeating units of the O-antigen oligosaccharide Of Escherichia coli serotype O56
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?
additional information
?
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no activity with N-butyryl-glucosamine-beta-1-thio-2-naphthyl as acceptor substrate
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?
additional information
?
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no activity with N-butyryl-glucosamine-beta-1-thio-2-naphthyl as acceptor substrate
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?
additional information
?
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no activity with N-butyryl-glucosamine-beta-1-thio-2-naphthyl as acceptor substrate
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?
additional information
?
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no activity with N-butyryl-glucosamine-beta-1-thio-2-naphthyl as acceptor substrate
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?
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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
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
the enzyme catalyzes the formation of the Glc-(1->3)-GlcNAc linkage in the repeating units of the O-antigen oligosaccharide of Escherichia coli serotype O152
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-
?
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
the enzyme catalyzes the formation of the Glc-1-3-GlcNAc linkage in the repeating units of the O-antigen oligosaccharide Of Escherichia coli serotype O56
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-
?
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
the enzyme catalyzes the formation of the Glc-(1->3)-GlcNAc linkage in the repeating units of the O-antigen oligosaccharide of Escherichia coli serotype O152
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-
?
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
the enzyme catalyzes the formation of the Glc-1-3-GlcNAc linkage in the repeating units of the O-antigen oligosaccharide Of Escherichia coli serotype O56
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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
cobalt(II)-acetate supports glucosyltransferase activity but much less than with MnCl2
Mg2+
both MnCl2 and MgCl2 are efficient activators at 5 mM concentration
Mn2+
both MnCl2 and MgCl2 are efficient activators at 5 mM concentration. The enzyme is fully active at MnCl2 concentrations between 0.5 and 25 mM
additional information
additional information
no activation by Ni2+, Cu2+, Pb2+, Zn2+, and Ca2+
additional information
no activation by Ni2+, Cu2+, Pb2+, Zn2+, and Ca2+
additional information
no activation by Ni2+, Cu2+, Pb2+, Zn2+, and Ca2+ significantly supported the glucosyltransferase activities
additional information
no activation by Ni2+, Cu2+, Pb2+, Zn2+, and Ca2+ significantly supported the glucosyltransferase activities
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Co2+
the addition of 5 mM Co2+ reduces the activation by 5 mM MnCl2 of the enzyme by 45%; the addition of 5 mM Co2+ reduces the activation by 5 mM MnCl2 of the enzyme by 76%
octyl-beta-D-glucoside
0.5%, 15% inhibition; 0.5%, 78% inhibition
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.14
UDP-alpha-D-glucose
pH 7.0, 37°C, assayed with bacterial membranes
0.5
UDP-alpha-D-glucose
pH 7.0, 37°C, assayed with bacterial membranes
additional information
N-acetyl-alpha-D-glucosaminyl-diphospho-11-phenoxyundecanol
it is not possible to determine the accurate Km and Vmax values for the standard acceptor substrate D-GlcNAc-alpha-diphospho-(CH2)11-O-Ph due to its hydrophobic character
additional information
N-acetyl-alpha-D-glucosaminyl-diphospho-11-phenoxyundecanol
it is not possible to determine the accurate Km and Vmax values for the standard acceptor substrate D-GlcNAc-alpha-diphospho-(CH2)11-O-Ph due to its hydrophobic character
additional information
N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
it is not possible to determine the accurate Km and Vmax values for the standard acceptor substrate N-acetyl-D-glucosaminyl-alpha-diphospho-11-phenoxyundecaprenol due to its hydrophobic character
additional information
N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
it is not possible to determine the accurate Km and Vmax values for the standard acceptor substrate N-acetyl-D-glucosaminyl-alpha-diphospho-11-phenoxyundecaprenol due to its hydrophobic character
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
5 - 9
pH 5.0: about 60% of maximal activity, pH 9.0: about 40% of maximal activity
5 - 9
pH 5.0: about 75% of maximal activity, pH 9.0: about 75% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (442 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified protein has no enzyme activity. The native enzyme is associated with membranes which may be essential for their function
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brockhausen, I.; Hu, B.; Liu, B.; Lau, K.; Szarek, W.A.; Wang, L.; Feng, L.
Characterization of two beta-1,3-glucosyltransferases from Escherichia coli serotypes O56 and O152
J. Bacteriol.
190
4922-4932
2008
Escherichia coli (B5L3F2), Escherichia coli (Q077R2), Escherichia coli serotype O56 (Q077R2), Escherichia coli serotype O152 (B5L3F2)
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