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Literature summary for 2.4.1.303 extracted from
- Acceptor substrate specificity of UDP-Gal:GlcNAc-R beta1,3-galactosyltransferase (WbbD) from Escherichia coli O7:K1 (2008), Glycoconj. J., 25, 663-673.
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | differences between mammalian and bacterial enzymes could be exploited in the design of specific glycosyltransferase inhibitors that block the synthesis of O-antigens | Escherichia coli |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | requirement for divalent metal ion | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UDP-alpha-D-galactose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol | Escherichia coli | the enzyme is involved O7 lipopolysaccharide biosynthesis | UDP + beta-D-Gal-beta-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol | - |
? |  |
| UDP-alpha-D-galactose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol | Escherichia coli VW187 (O7:K1) | the enzyme is involved O7 lipopolysaccharide biosynthesis | UDP + beta-D-Gal-beta-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | Q03084 | - |
- |
| Escherichia coli VW187 (O7:K1) | Q03084 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | WbbD require at least one phosphate in the acceptor substrate which has to be directly linked to GlcNAc, and ise optimally active when GlcNAc is linked to diphosphate. No glycosyl transfer is observed with cytidine-monophosphate N-acetylneuraminic acid, UDP-GalNAc, GDP-Man or UDP-GlcNAc. WbbD does not recognize GlcNAc linked to a glycopeptide | Escherichia coli | ? | - |
? | |
| additional information | WbbD require at least one phosphate in the acceptor substrate which has to be directly linked to GlcNAc, and ise optimally active when GlcNAc is linked to diphosphate. No glycosyl transfer is observed with cytidine-monophosphate N-acetylneuraminic acid, UDP-GalNAc, GDP-Man or UDP-GlcNAc. WbbD does not recognize GlcNAc linked to a glycopeptide | Escherichia coli VW187 (O7:K1) | ? | - |
? | |
| UDP-alpha-D-galactose + 1-O-(11-phenoxyundecyl-diphosphoryl)-alpha-D-glucopyranoside | synthetic substrate, which is an analog of N-acetyl-D-glucosaminyldiphospho-ditrans,octacis-undecaprenol. The enzyme does not require a specific length of the lipid chain but can act on GlcNAc-alpha-PO3-PO3-(CH2)R-OPh substrates where R can be 6, 11 or 16 carbons | Escherichia coli | UDP + 1-O-(11-phenoxyundecyl-diphosphoryl)-3-O-beta-D-galactopyranosyl-alpha-D-glucopyranoside | - |
? | |
| UDP-alpha-D-galactose + 1-O-(11-phenoxyundecyl-diphosphoryl)-alpha-D-glucopyranoside | synthetic substrate, which is an analog of N-acetyl-D-glucosaminyldiphospho-ditrans,octacis-undecaprenol. The enzyme does not require a specific length of the lipid chain but can act on GlcNAc-alpha-PO3-PO3-(CH2)R-OPh substrates where R can be 6, 11 or 16 carbons | Escherichia coli VW187 (O7:K1) | UDP + 1-O-(11-phenoxyundecyl-diphosphoryl)-3-O-beta-D-galactopyranosyl-alpha-D-glucopyranoside | - |
? | |
| UDP-alpha-D-galactose + 1-O-(16-phenoxyhexadecyl-diphosphoryl)-alpha-D-glucopyranoside | synthetic substrate, which is an analog of N-acetyl-D-glucosaminyldiphospho-ditrans,octacis-undecaprenol. The enzyme does not require a specific length of the lipid chain but can act on GlcNAc-alpha-PO3-PO3-(CH2)R-OPh substrates where R can be 6, 11 or 16 carbons | Escherichia coli | UDP + 1-O-(16-phenoxyhexadecyl-diphosphoryl)-3-O-beta-D-galactopyranosyl-alpha-D-glucopyranoside | - |
? | |
| UDP-alpha-D-galactose + 1-O-(16-phenoxyhexadecyl-diphosphoryl)-alpha-D-glucopyranoside | synthetic substrate, which is an analog of N-acetyl-D-glucosaminyldiphospho-ditrans,octacis-undecaprenol. The enzyme does not require a specific length of the lipid chain but can act on GlcNAc-alpha-PO3-PO3-(CH2)R-OPh substrates where R can be 6, 11 or 16 carbons | Escherichia coli VW187 (O7:K1) | UDP + 1-O-(16-phenoxyhexadecyl-diphosphoryl)-3-O-beta-D-galactopyranosyl-alpha-D-glucopyranoside | - |
? | |
| UDP-alpha-D-galactose + 1-O-(6-phenoxyhex-1-yl-diphosphoryl)-alpha-D-glucopyranoside | synthetic substrate, which is an analog of N-acetyl-D-glucosaminyldiphospho-ditrans,octacis-undecaprenol. The enzyme does not require a specific length of the lipid chain but can act on GlcNAc-alpha-PO3-PO3-(CH2)R-OPh substrates where R can be 6, 11 or 16 carbons | Escherichia coli | UDP + 1-O-(6-phenoxyhexadecyl-diphosphoryl)-3-O-beta-D-galactopyranosyl-alpha-D-glucopyranoside | - |
? | |
| UDP-alpha-D-galactose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol | the enzyme is involved O7 lipopolysaccharide biosynthesis | Escherichia coli | UDP + beta-D-Gal-beta-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol | - |
? | |
| UDP-alpha-D-galactose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol | the enzyme is specific for UDP-galactose as donor substrate | Escherichia coli | UDP + beta-D-Gal-beta-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol | - |
? | |
| UDP-alpha-D-galactose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol | the enzyme is involved O7 lipopolysaccharide biosynthesis | Escherichia coli VW187 (O7:K1) | UDP + beta-D-Gal-beta-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol | - |
? | |
| UDP-alpha-D-galactose + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol | the enzyme is specific for UDP-galactose as donor substrate | Escherichia coli VW187 (O7:K1) | UDP + beta-D-Gal-beta-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| UDP-Gal:GlcNAc-R beta1,3-galactosyltransferase | - |
Escherichia coli |
| WbbD | - |
Escherichia coli |
| WbbD beta3Gal-transferase | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the enzyme is essential for O antigen synthesis in the VW187 strain | Escherichia coli |
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