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Literature summary for 2.7.7.23 extracted from
- The Mechanism of acetyl transfer catalyzed by Mycobacterium tuberculosis GlmU (2018), Biochemistry, 57, 3387-3401 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| apo GlmU is crystallized at 20 °C using the sitting-drop vapor diffusion methodcrystal structure of a mimic of the Michaelis complex, with glucose 1-phosphate and acetyl-coenzyme A, helps us to propose the residues involved in deprotonation of glucosamine 1-phosphate and the loop movement that likely generates the active site required for glucosamine 1-phosphate to bind | Mycobacterium tuberculosis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.008 | - |
UTP | pH 7.5, 30°C | Mycobacterium tuberculosis |  |
| 0.03 | - |
N-acetyl-alpha-D-glucosamine 1-phosphate | pH 7.5, 30°C | Mycobacterium tuberculosis | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | activates | Mycobacterium tuberculosis | |
| Mg2+ | required | Mycobacterium tuberculosis | |
| Mn2+ | activates | Mycobacterium tuberculosis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | Mycobacterium tuberculosis | - |
diphosphate + UDP-N-acetyl-alpha-D-glucosamine | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | A5U161 | - |
- |
| Mycobacterium tuberculosis ATCC 25177 | A5U161 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Mycobacterium tuberculosis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
Mycobacterium tuberculosis | diphosphate + UDP-N-acetyl-alpha-D-glucosamine | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| bifunctional N-acetyltransferase/uridylyltransferase | - |
Mycobacterium tuberculosis |
| GlmU | bifunctional enzyme, also to possess the activity of EC 2.7.7.157, glucosamine-1-phosphate N-acetyltransferase | Mycobacterium tuberculosis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Mycobacterium tuberculosis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 100 | - |
N-acetyl-alpha-D-glucosamine 1-phosphate | pH 7.5, 30°C | Mycobacterium tuberculosis | |
| 120 | - |
UTP | pH 7.5, 30°C | Mycobacterium tuberculosis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Mycobacterium tuberculosis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the bifunctional enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan | Mycobacterium tuberculosis |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 3333 | - |
N-acetyl-alpha-D-glucosamine 1-phosphate | pH 7.5, 30°C | Mycobacterium tuberculosis | |
| 15000 | - |
UTP | pH 7.5, 30°C | Mycobacterium tuberculosis | |
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Release 2023.1 (January 2023)
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