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Literature summary extracted from

  • 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 (2008), J. Bacteriol., 190, 4922-4932.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.305
-
Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.305 CHAPS 0.5%, 41% inhibition; 0.5%, 75% inhibition Escherichia coli
2.4.1.305 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% Escherichia coli
2.4.1.305 EDTA
-
Escherichia coli
2.4.1.305 octyl-beta-D-glucoside 0.5%, 15% inhibition; 0.5%, 78% inhibition Escherichia coli
2.4.1.305 Triton X-100
-
Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.305 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 Escherichia coli
2.4.1.305 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 Escherichia coli
2.4.1.305 0.14
-
UDP-alpha-D-glucose pH 7.0, 37°C, assayed with bacterial membranes Escherichia coli
2.4.1.305 0.5
-
UDP-alpha-D-glucose pH 7.0, 37°C, assayed with bacterial membranes Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.305 membrane
-
Escherichia coli 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.305 Co2+ cobalt(II)-acetate supports glucosyltransferase activity but much less than with MnCl2 Escherichia coli
2.4.1.305 Mg2+ both MnCl2 and MgCl2 are efficient activators at 5 mM concentration Escherichia coli
2.4.1.305 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 Escherichia coli
2.4.1.305 additional information no activation by Ni2+, Cu2+, Pb2+, Zn2+, and Ca2+ Escherichia coli
2.4.1.305 additional information no activation by Ni2+, Cu2+, Pb2+, Zn2+, and Ca2+ significantly supported the glucosyltransferase activities Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.1.305 55000
-
SDS-PAGE Escherichia coli
2.4.1.305 55400
-
SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.305 UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol Escherichia coli 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 UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
-
?
2.4.1.305 UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol Escherichia coli 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 UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
-
?
2.4.1.305 UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol Escherichia coli serotype O56 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 UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
-
?
2.4.1.305 UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol Escherichia coli serotype O152 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 UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.305 Escherichia coli B5L3F2
-
-
2.4.1.305 Escherichia coli Q077R2
-
-
2.4.1.305 Escherichia coli serotype O152 B5L3F2
-
-
2.4.1.305 Escherichia coli serotype O56 Q077R2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.305 purified protein has no enzyme activity. The native enzyme is associated with membranes which may be essential for their function Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.1.305 0.0022
-
pH 7.0, 37°C, assayed with bacterial membranes Escherichia coli
2.4.1.305 0.025
-
pH 7.0, 37°C, assayed with bacterial membranes Escherichia coli

Storage Stability

EC Number Storage Stability Organism
2.4.1.305 -20°C, stable for several weeks Escherichia coli
2.4.1.305 4°C, stable for several days Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.305 additional information no activity with N-butyryl-glucosamine-beta-1-thio-2-naphthyl as acceptor substrate Escherichia coli ?
-
?
2.4.1.305 additional information no activity with N-butyryl-glucosamine-beta-1-thio-2-naphthyl as acceptor substrate Escherichia coli serotype O56 ?
-
?
2.4.1.305 additional information no activity with N-butyryl-glucosamine-beta-1-thio-2-naphthyl as acceptor substrate Escherichia coli serotype O152 ?
-
?
2.4.1.305 UDP-alpha-D-glucose + alpha-D-GlcNAc-diphospho-(CH2)9-CH3 150% of the activity compared to N-acetyl-alpha-D-glucosaminyl-diphospho-11-phenoxyundecaprenol as acceptor substrate Escherichia coli UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-(CH2)9-CH3
-
?
2.4.1.305 UDP-alpha-D-glucose + alpha-D-GlcNAc-diphospho-(CH2)9-CH3 150% of the activity compared to N-acetyl-alpha-D-glucosaminyl-diphospho-11-phenoxyundecaprenol as acceptor substrate Escherichia coli serotype O152 UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-(CH2)9-CH3
-
?
2.4.1.305 UDP-alpha-D-glucose + alpha-D-GlcNAc-diphospho-16-phenoxyhexadecanol
-
Escherichia coli UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-16-phenoxyhexadecanol
-
?
2.4.1.305 UDP-alpha-D-glucose + alpha-D-GlcNAc-diphospho-16-phenoxyhexadecanol
-
Escherichia coli serotype O152 UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-16-phenoxyhexadecanol
-
?
2.4.1.305 UDP-alpha-D-glucose + alpha-D-GlcNAc-diphospho-6-phenoxyhexanol
-
Escherichia coli UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-6-phenoxyhexanol
-
?
2.4.1.305 UDP-alpha-D-glucose + alpha-D-GlcNAc-diphospho-6-phenoxyhexanol
-
Escherichia coli serotype O152 UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-6-phenoxyhexanol
-
?
2.4.1.305 UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-(CH2)9-CH3 32% of the activity compared to N-acetyl-alpha-D-glucosaminyl-diphospho-11-phenoxyundecaprenol as acceptor substrate Escherichia coli UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-(CH2)9-CH3
-
?
2.4.1.305 UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-(CH2)9-CH3 32% of the activity compared to N-acetyl-alpha-D-glucosaminyl-diphospho-11-phenoxyundecaprenol as acceptor substrate Escherichia coli serotype O56 UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-(CH2)9-CH3
-
?
2.4.1.305 UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-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 Escherichia coli UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-11-phenoxyundecanol
-
?
2.4.1.305 UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-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 Escherichia coli UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-11-phenoxyundecanol
-
?
2.4.1.305 UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-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 Escherichia coli serotype O56 UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-11-phenoxyundecanol
-
?
2.4.1.305 UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-16-phenoxyhexadecanol
-
Escherichia coli UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-16-phenoxyhexadecanol
-
?
2.4.1.305 UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-16-phenoxyhexadecanol
-
Escherichia coli serotype O56 UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-16-phenoxyhexadecanol
-
?
2.4.1.305 UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-diphospho-6-phenoxyhexanol
-
Escherichia coli UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-6-phenoxyhexanol
-
?
2.4.1.305 UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-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 Escherichia coli UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
-
?
2.4.1.305 UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-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 Escherichia coli UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
-
?
2.4.1.305 UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-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 Escherichia coli serotype O56 UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
-
?
2.4.1.305 UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosaminyl-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 Escherichia coli serotype O152 UDP + beta-D-Glc-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
-
?

Subunits

EC Number Subunits Comment Organism
2.4.1.305 ? x * 55000, SDS-PAGE Escherichia coli
2.4.1.305 ? x * 55400, SDS-PAGE Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.4.1.305 UDP-Glc:GlcNAc-pyrophosphate-lipid beta-1,3-glucosyltransferase
-
Escherichia coli
2.4.1.305 WfaP
-
Escherichia coli
2.4.1.305 WfgD
-
Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.305 37
-
assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.305 6
-
-
Escherichia coli
2.4.1.305 6.5
-
-
Escherichia coli
2.4.1.305 7
-
assay at Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.4.1.305 5 9 pH 5.0: about 60% of maximal activity, pH 9.0: about 40% of maximal activity Escherichia coli
2.4.1.305 5 9 pH 5.0: about 75% of maximal activity, pH 9.0: about 75% of maximal activity Escherichia coli