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Literature summary for 2.3.1.157 extracted from
- Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis (1994), J. Bacteriol., 176, 5788-5795.
General Stability
| General Stability | Organism |
|---|---|
| acetyltransferase activity rapidly lost when the enzyme is stored in the absence of reducing thiols or acetyl coenzyme A or is treated with thiol-alkylating agents | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 2-Nitro-5-thiocyanobenzoic acid | - |
Escherichia coli |  |
| DTNB | - |
Escherichia coli | |
| N-acetylglucosamine-1-phosphate | acetyltransferase activity inhibited by its reaction product | Escherichia coli | |
| UDP-MurNAc | 1 mM, relative enzyme activity 2% | Escherichia coli | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.07 | - |
N-acetyl-D-glucosamine 1-phosphate | uridyltransferase activity | Escherichia coli | |
| 0.1 | - |
UTP | uridyltransferase activity | Escherichia coli | |
| 0.15 | - |
D-glucosamine 1-phosphate | - |
Escherichia coli | |
| 0.6 | - |
acetyl-CoA | - |
Escherichia coli | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | absolute requirement for both activities in the sharp range from 1-10 mM with an optimal value of 3 mM | Escherichia coli | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 49000 | - |
gel filtration | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glucosamine 1-phosphate + acetyl-CoA | Bacillus subtilis | - |
N-acetyl-D-glucosamine 1-phosphate + CoA | - |
? | |
| D-glucosamine 1-phosphate + acetyl-CoA | Escherichia coli | - |
N-acetyl-D-glucosamine 1-phosphate + CoA | - |
? | |
| D-glucosamine 1-phosphate + acetyl-CoA | Escherichia coli JM83 | - |
N-acetyl-D-glucosamine 1-phosphate + CoA | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | - |
- |
- |
| Escherichia coli | - |
JM83 | - |
| Escherichia coli JM83 | - |
JM83 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| GlmU gene product, bifunctional enzyme with glucosamine-1-phosphate acetyltransferase and uridyltransferase activity | Escherichia coli |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | the enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase | Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 2.2 | - |
GlcN-1-P acetyltransferase activity | Escherichia coli |
| 15.1 | - |
GlcNAc-1-P uridyltransferase activity | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glucosamine 1-phosphate + acetyl-CoA | - |
Bacillus subtilis | N-acetyl-D-glucosamine 1-phosphate + CoA | - |
? | |
| D-glucosamine 1-phosphate + acetyl-CoA | - |
Escherichia coli | N-acetyl-D-glucosamine 1-phosphate + CoA | - |
? | |
| D-glucosamine 1-phosphate + acetyl-CoA | - |
Escherichia coli JM83 | N-acetyl-D-glucosamine 1-phosphate + CoA | - |
? | |
| N-acetyl-D-glucosamine 1-phosphate + UTP | - |
Bacillus subtilis | UDP-N-acetylglucosamine + ? | - |
? | |
| N-acetyl-D-glucosamine 1-phosphate + UTP | glmU gene product, bifunctional enzyme catalyzing 2 subsequent steps in the pathway for UDP-GlcNAc synthesis | Escherichia coli | UDP-N-acetylglucosamine + ? | - |
r | |
| N-acetyl-D-glucosamine 1-phosphate + UTP | glmU gene product, bifunctional enzyme catalyzing 2 subsequent steps in the pathway for UDP-GlcNAc synthesis | Escherichia coli JM83 | UDP-N-acetylglucosamine + ? | - |
r | |
| UDP-N-acetyl-alpha-D-glucosamine + H2O | - |
Escherichia coli | N-acetyl-D-glucosamine 1-phosphate + UMP | - |
r | |
| UDP-N-acetyl-alpha-D-glucosamine + H2O | - |
Escherichia coli JM83 | N-acetyl-D-glucosamine 1-phosphate + UMP | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| trimer | 2 * 49000 or 3 * 49000, dimer or trimer of identical subunits, gel filtration | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GlmU enzyme | - |
Escherichia coli |
| GlmU uridyltransferase | - |
Escherichia coli |
| UDP-GlcNAc pyrophosphorylase | - |
Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 12.4 | - |
N-acetyl-D-glucosamine 1-phosphate | GmlU uridyltransferase | Escherichia coli | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.2 | - |
for both acetyltransferase and uridyltransferase | Escherichia coli |
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