Information on EC 2.4.1.305 - UDP-Glc:alpha-D-GlcNAc-glucosaminyl-diphosphoundecaprenol beta-1,3-glucosyltransferase

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
2.4.1.305
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RECOMMENDED NAME
GeneOntology No.
UDP-Glc:alpha-D-GlcNAc-glucosaminyl-diphosphoundecaprenol beta-1,3-glucosyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
UDP-alpha-D-glucose + alpha-D-GlcNAc-diphospho-16-phenoxyhexadecanol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-16-phenoxyhexadecanol
show the reaction diagram
UDP-alpha-D-glucose + alpha-D-GlcNAc-diphospho-6-phenoxyhexanol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-6-phenoxyhexanol
show the reaction diagram
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
show the reaction diagram
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-11-phenoxyundecanol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-11-phenoxyundecanol
show the reaction diagram
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-16-phenoxyhexadecanol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-16-phenoxyhexadecanol
show the reaction diagram
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-6-phenoxyhexanol
UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-6-phenoxyhexanol
show the reaction diagram
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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
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
cobalt(II)-acetate supports glucosyltransferase activity but much less than with MnCl2; cobalt(II)-acetate supports glucosyltransferase activity but much less than with MnCl2
Mg2+
both MnCl2 and MgCl2 are efficient activators at 5 mM concentration; 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; 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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CHAPS
0.5%, 41% inhibition; 0.5%, 75% inhibition
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.14 - 0.5
UDP-alpha-D-glucose
additional information
N-acetyl-alpha-D-glucosaminyl-diphospho-11-phenoxyundecanol
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0022
pH 7.0, 37C, assayed with bacterial membranes
0.025
pH 7.0, 37C, assayed with bacterial membranes
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
assay at; assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
pH 5.0: about 60% of maximal activity, pH 9.0: about 40% of maximal activity; pH 5.0: about 75% of maximal activity, pH 9.0: about 75% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at; assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for several weeks
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4C, stable for several days
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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; purified protein has no enzyme activity. The native enzyme is associated with membranes which may be essential for their function
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE