Information on EC 2.4.1.304 - UDP-Gal:alpha-D-GlcNAc-diphosphoundecaprenol beta-1,4-galactosyltransferase

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The expected taxonomic range for this enzyme is: Shigella boydii

EC NUMBER
COMMENTARY hide
2.4.1.304
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RECOMMENDED NAME
GeneOntology No.
UDP-Gal:alpha-D-GlcNAc-diphosphoundecaprenol beta-1,4-galactosyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-galactose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + beta-D-Gal-(1->4)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-galactose:N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol beta-1,4-galactosyltransferase
The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Shigella boydii B14. The activity is stimulated by Mn2+ or to a lesser extent by Mg2+, Ca2+, Ni2+ or Pb2+.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
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Manually annotated by BRENDA team
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-galactose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
UDP + beta-D-Gal-(1->4)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
show the reaction diagram
UDP-alpha-D-galactose + N-acetyl-alpha-D-glucosaminyl-diphospho-hexadecanol
UDP + beta-D-Gal-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-hexadecanol
show the reaction diagram
UDP-alpha-D-galactose + N-acetyl-alpha-D-glucosaminyl-diphospho-hexanol
UDP + beta-D-Gal-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-hexanol
show the reaction diagram
UDP-alpha-D-galactose + N-acetyl-alpha-D-glucosaminyl-diphospho-phenoxyundecanol
UDP + beta-D-Gal-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-phenoxyundecanol
show the reaction diagram
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the synthetic acceptor substrate D-GlcNAc-alpha-PP-(CH2)11-O-Ph is an amphipathic molecule with similarity to the endogenous substrate D-GlcNAc-alpha-diphospho-ditrans,octacis-undecaprenol. The enzyme requires diphosphate in the acceptor substrate, Strict specificity for UDP-D-galactose as donor substrate
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?
UDP-alpha-D-galactose + N-acetyl-alpha-D-glucosaminyl-diphosphononanol
UDP + beta-D-Gal-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphononanol
show the reaction diagram
UDP-alpha-D-galactose + N-acetyl-alpha-D-glucosaminyl-phospho-phenoxyundecanol
UDP + beta-D-Gal-(1->4)-N-acetyl-alpha-D-glucosaminyl-phospho-phenoxyundecanol
show the reaction diagram
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synthetic acceptor. 11% of the activity with N-acetyl-D-glucosaminyl-alpha-diphospho-phenoxyundecanol
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?
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-galactose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
UDP + beta-D-Gal-(1->4)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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5 mM, highest stimulation of activity in the presence of Mn2+. Ca2+, Pb2+, Ni2+ and Mg2+ are also effective
Mg2+
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5 mM, highest stimulation of activityN in the presence of Mn2+. Ca2+, Pb2+, Ni2+ and Mg2+ are also effective
Mn2+
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5 mM, highest stimulation of activity in the presence of Mn2+. Ca2+, Pb2+, Ni2+ and Mg2+ are also effective
Ni2+
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5 mM, highest stimulation of activity in the presence of Mn2+. Ca2+, Pb2+, Ni2+ and Mg2+ are also effective
Pb2+
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5 mM, highest stimulation of activity in the presence of Mn2+. Ca2+, Pb2+, Ni2+ and Mg2+ are also effective
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-hydroxyphenylglyoxal
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0.2 mM, 50% inhibition
5,5'-dithio-bis-2-nitrobenzoic acid
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0.2 mM, 85% inhibition
diethyl dicarbonate
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0.2 mM 31% inhibition
Triton X-100
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as the concentration of Triton X-100 increases from 0 to 0.5% in the reaction mixture, the activity of the enzyme decreases but is maintained at about 60% of the original activity, up to 6% Triton X-100
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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1-30 mM, 4fold-stimulation
dithiothreitol
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0.1-3 mM, about 5fold stimulation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
N-acetyl-alpha-D-glucosaminyl-diphospho-phenoxyundecanol
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pH 7, 37°C
0.25
UDP-alpha-D-galactose
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pH 7, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
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SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, the crude enzyme preparation retains at least 60% of the initial activity after storage for up to 9 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D99A
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highly active mutant enzyme
E101A
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mutant exhibits minimal enzyme activity, greatly reduced enzyme activity in the presence of either Mn2+ or Pb2+
E103A
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highly active mutant enzyme
K211A
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greatly reduced activity, 60fold higher activity in the presence of Pb2+ than in the presence of Mn2+
R210A
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active mutant enzyme
R212A
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active mutant enzyme
D99A
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highly active mutant enzyme
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E101A
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mutant exhibits minimal enzyme activity, greatly reduced enzyme activity in the presence of either Mn2+ or Pb2+
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E103A
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highly active mutant enzyme
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R210A
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active mutant enzyme
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R212A
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active mutant enzyme
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