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Literature summary for 2.3.1.157 extracted from
- Kinetic modelling of GlmU reactions - prioritization of reaction for therapeutic application (2012), PLoS ONE, 7, e43969.
Application
| Application | Comment | Organism |
|---|---|---|
| drug development | due to developed resistance against the existing anti-tubercular drugs by Mycobacteriumm tuberculosis, the enzyme is a target for drug development. Targeting uridyltranferase activity of Mtu GlmU would be a better choice for therapeutic intervention, since at low metabolite concentrations, inhibition of either of the GlmU reactions cause significant decrement in the overall GlmU rate, but at higher metabolite concentrations, uridyltransferase inhibition shows higher decrement, overview | Mycobacterium tuberculosis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | modelling of competitive and uncompetitive inhibition of Rxn-1 by substrates/products, overview | Mycobacterium tuberculosis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic modelling of GlmU, simulation of the model, detailed overview. Estimated and measured values are very coherent | Mycobacterium tuberculosis | |
| 0.000009 | - |
CoA | pH 7.5, 25°C | Mycobacterium tuberculosis |  |
| 0.003 | - |
N-acetyl-alpha-D-glucosamine 1-phosphate | pH 7.5, 25°C | Mycobacterium tuberculosis | |
| 0.061 | - |
alpha-D-glucosamine 1-phosphate | pH 7.5, 25°C | Mycobacterium tuberculosis | |
| 0.224 | - |
acetyl-CoA | pH 7.5, 25°C | Mycobacterium tuberculosis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + alpha-D-glucosamine 1-phosphate | Mycobacterium tuberculosis | - |
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | - |
gene rxn-1 | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | both reactions of bifunctional GlmU follow Michaelis Menten ordered bi-bi mechanism involving an obligatory order of binding of substrates to the enzyme | Mycobacterium tuberculosis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + alpha-D-glucosamine 1-phosphate | - |
Mycobacterium tuberculosis | CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GlmU | - |
Mycobacterium tuberculosis |
| glucosamine 1-phosphate N-acetyltransferase/N-acetylglucosamine-1-phosphate uridyltransferase | - |
Mycobacterium tuberculosis |
| Rxn-1 | - |
Mycobacterium tuberculosis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Mycobacterium tuberculosis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Mycobacterium tuberculosis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the C- and N-terminal domains of bifunctional enzyme mycobacterial glucosamine 1-phosphate N-acetyltransferase/N-acetylglucosamine-1-phosphate uridyltransferase catalyze acetyltransferase and uridyltransferase (cf. EC 2.7.7.23) activities, respectively, and the final product is involved in peptidoglycan synthesis | Mycobacterium tuberculosis |
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