Any feedback?
Literature summary for 2.4.1.132 extracted from
- Identification and biochemical characterization of a novel alpha-1,3-mannosyltransferase WfcD from Escherichia coli O141 (2017), Carbohydr. Res., 443-444, 78-86 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | - |
Escherichia coli |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene wfcD, included in the O-antigen repeating unit and O-antigen biosynthesis of Escherichia coli strain O141, genetic structure of the gene cluster, overview. Functional recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | - |
Escherichia coli | |
| Cu2+ | - |
Escherichia coli | |
| Ni2+ | - |
Escherichia coli | |
| Zn2+ | - |
Escherichia coli | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.56 | - |
GDP-alpha-D-mannose | pH 7.0, 37°C, recombinant enzyme | Escherichia coli | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | activates | Escherichia coli | |
| Mg2+ | activates | Escherichia coli | |
| Mn2+ | activates | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GDP-alpha-D-mannose + D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol | Escherichia coli | - |
GDP + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol | - |
? | |
| GDP-alpha-D-mannose + D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol | Escherichia coli O141 | - |
GDP + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | A6MF03 | - |
- |
| Escherichia coli O141 | A6MF03 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GDP-alpha-D-mannose + D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol | - |
Escherichia coli | GDP + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol | - |
? | |
| GDP-alpha-D-mannose + D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol | - |
Escherichia coli O141 | GDP + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol | - |
? | |
| GDP-alpha-D-mannose + decyl diphosphate 2-acetamido-2-deoxy-alpha-D-glucopyranose | i.e. synthetic acceptor GlcNAc-PP-De | Escherichia coli | GDP + ? | - |
? | |
| GDP-alpha-D-mannose + decyl diphosphate 2-acetamido-2-deoxy-alpha-D-glucopyranose | i.e. synthetic acceptor GlcNAc-PP-De | Escherichia coli O141 | GDP + ? | - |
? | |
| GDP-alpha-D-mannose + P1-[11- (anthracen-9-ylmethoxy) undecyl]-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl) diphosphate | i.e. GlcNAc-PP-AnthrU | Escherichia coli | GDP + ? | - |
? | |
| GDP-alpha-D-mannose + P1-[11- (anthracen-9-ylmethoxy) undecyl]-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl) diphosphate | i.e. GlcNAc-PP-AnthrU | Escherichia coli O141 | GDP + ? | - |
? | |
| additional information | enzyme WfcD is expressed in Escherichia coli strain BL21(DE3), and the enzymatic product is identified by liquid chromatography-mass spectrometry (LC-MS), collision-induced dissociation electrospray ionization ion trap multiple tandem MS (CID-ESI-IT-MSn), and glycosidase digestion using the donor substrate GDP-Man and the synthetic acceptor substrate decyl diphosphate 2-acetamido-2-deoxy-alpha-D-glucopyranose (GlcNAc-PP-De). Analysis of donor substrate specificity of WfcD, overview. WfcD is an alpha-1,3-ManT that catalyzes the Man(alpha1-3)-GlcNAc-R linkage formation. No activity with GlcNAc-GlcNAc-PP-De, Glc-PP-De, UDP-GlcNAc, GlcNAc, and GlcNAc-NP | Escherichia coli | ? | - |
- |
|
| additional information | enzyme WfcD is expressed in Escherichia coli strain BL21(DE3), and the enzymatic product is identified by liquid chromatography-mass spectrometry (LC-MS), collision-induced dissociation electrospray ionization ion trap multiple tandem MS (CID-ESI-IT-MSn), and glycosidase digestion using the donor substrate GDP-Man and the synthetic acceptor substrate decyl diphosphate 2-acetamido-2-deoxy-alpha-D-glucopyranose (GlcNAc-PP-De). Analysis of donor substrate specificity of WfcD, overview. WfcD is an alpha-1,3-ManT that catalyzes the Man(alpha1-3)-GlcNAc-R linkage formation. No activity with GlcNAc-GlcNAc-PP-De, Glc-PP-De, UDP-GlcNAc, GlcNAc, and GlcNAc-NP | Escherichia coli O141 | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 44500, about, sequence calculation, x * 45000, recombinant His6-tagged enzyme, SDS-PAGE | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| alpha-1,3-mannosyltransferase | - |
Escherichia coli |
| alpha-1,3-ManT | - |
Escherichia coli |
| WfcD | - |
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 | - |
recombinant enzyme | Escherichia coli |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 9 | activity range, donor substrate specificity, profile overview | Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | WfcD is the first characterized bacterial mannosyltransferase that acts on the Man-alpha-(1->3)-GlcNAc linkage | Escherichia coli |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
