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Literature summary for 2.3.1.157 extracted from
- Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) inhibitory activity of terreic acid isolated from Aspergillus terreus (2016), J. Biomol. Screen., 21, 342-353 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene glmU, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Haemophilus influenzae |
| gene glmU, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenylamino]-2-(-4-pyridyl)-1-ethanone | commercial inhibitor | Escherichia coli |  |
| 1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenylamino]-2-(-4-pyridyl)-1-ethanone | commercial inhibitor | Haemophilus influenzae | |
| terreic acid | terreic acid inhibits the glucosamine-1-phosphate-acetyltransferase activity of the bifunctional enzyme. Mode of inhibition studies reveal that terreic acid is competitive with AcCoA and uncompetitive with GlcN-1-phosphate. It also exhibits concentration-dependent killing of Escherichia coli strain ATCC 25922 and inhibits the growth of biofilms generated by Escherichia coli. GlmU acetyltransferase is a molecular target of terreic acid, resulting in its antibacterial activity. Terreic acid is isolated from Aspergillus terreus strain MRCJ-356. Molecular modeling, MIC value | Escherichia coli | |
| terreic acid | terreic acid inhibits the glucosamine-1-phosphate-acetyltransferase activity of the bifunctional enzyme. Mode of inhibition studies reveal that terreic acid is competitive with AcCoA and uncompetitive with GlcN-1-phosphate. It also exhibits concentration-dependent killing of Escherichia coli strain ATCC 25922 and inhibits the growth of biofilms generated by Escherichia coli. GlmU acetyltransferase is a molecular target of terreic acid, resulting in its antibacterial activity. Terreic acid is isolated from Aspergillus terreus strain MRCJ-356. Molecular modeling | Haemophilus influenzae | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Haemophilus influenzae | |
| Mg2+ | required | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + alpha-D-glucosamine 1-phosphate | Haemophilus influenzae | - |
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
| acetyl-CoA + alpha-D-glucosamine 1-phosphate | Escherichia coli | - |
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
| acetyl-CoA + alpha-D-glucosamine 1-phosphate | Escherichia coli ATCC 25922 | - |
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0ACC7 | - |
- |
| Escherichia coli ATCC 25922 | P0ACC7 | - |
- |
| Haemophilus influenzae | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Haemophilus influenzae |
| recombinant His-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. |
|---|---|---|---|---|---|---|
| acetyl-CoA + alpha-D-glucosamine 1-phosphate | - |
Haemophilus influenzae | CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
| acetyl-CoA + alpha-D-glucosamine 1-phosphate | - |
Escherichia coli | CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
| acetyl-CoA + alpha-D-glucosamine 1-phosphate | - |
Escherichia coli ATCC 25922 | CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GlmU | - |
Haemophilus influenzae |
| GlmU | - |
Escherichia coli |
| More | bifunctional enzyme, cf. EC 2.7.7.23 | Haemophilus influenzae |
| More | bifunctional enzyme, cf. EC 2.7.7.23 | Escherichia coli |
| N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase | - |
Haemophilus influenzae |
| N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Haemophilus influenzae |
| 30 | - |
assay at | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.6 | - |
assay at | Haemophilus influenzae |
| 7.6 | - |
assay at | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| acetyl-CoA | - |
Haemophilus influenzae | |
| acetyl-CoA | - |
Escherichia coli | |
IC50 Value
| IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|
| 0.04424 | - |
pH 7.6, 30°C, recombinant enzyme | Escherichia coli | terreic acid | |
| 0.09756 | - |
pH 7.6, 30°C | Haemophilus influenzae | terreic acid | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | pathway and metabolism of UDP-N-acetylglucosamine in prokaryotes and eukaryotes, overview | Haemophilus influenzae |
| metabolism | pathway and metabolism of UDP-N-acetylglucosamine in prokaryotes and eukaryotes, overview | Escherichia coli |
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