EC Number | Cloned (Comment) | Organism |
---|---|---|
2.7.7.23 | overexpression in host strain | Escherichia coli |
EC Number | General Stability | Organism |
---|---|---|
2.3.1.157 | 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 |
2.7.7.23 | completely insensitive to millimolar concentrations of thiol reagents | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.157 | 2-Nitro-5-thiocyanobenzoic acid | - |
Escherichia coli | |
2.3.1.157 | DTNB | - |
Escherichia coli | |
2.3.1.157 | N-acetylglucosamine-1-phosphate | acetyltransferase activity inhibited by its reaction product | Escherichia coli | |
2.3.1.157 | UDP-MurNAc | 1 mM, relative enzyme activity 2% | Escherichia coli | |
2.7.7.23 | UDP-N-acetyl-D-glucosamine | slight product inhibition in reverse reaction | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.157 | 0.07 | - |
N-acetyl-D-glucosamine 1-phosphate | uridyltransferase activity | Escherichia coli | |
2.3.1.157 | 0.1 | - |
UTP | uridyltransferase activity | Escherichia coli | |
2.3.1.157 | 0.15 | - |
D-glucosamine 1-phosphate | - |
Escherichia coli | |
2.3.1.157 | 0.6 | - |
acetyl-CoA | - |
Escherichia coli | |
2.7.7.23 | 0.07 | - |
N-acetyl-D-glucosamine 1-phosphate | pH 8.2, 37°C | Escherichia coli | |
2.7.7.23 | 0.1 | - |
UTP | pH 8.2, 37°C | Escherichia coli |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.157 | Mg2+ | absolute requirement for both activities in the sharp range from 1-10 mM with an optimal value of 3 mM | Escherichia coli | |
2.7.7.23 | Mg2+ | required for maximum activity | Escherichia coli | |
2.7.7.23 | Mg2+ | optimum activity at 3 mM | Escherichia coli |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.3.1.157 | 49000 | - |
gel filtration | Escherichia coli |
2.7.7.23 | 49000 | - |
SDS-PAGE, corresponds very well with molecular weight expected from DNA sequence | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.157 | D-glucosamine 1-phosphate + acetyl-CoA | Bacillus subtilis | - |
N-acetyl-D-glucosamine 1-phosphate + CoA | - |
? | |
2.3.1.157 | D-glucosamine 1-phosphate + acetyl-CoA | Escherichia coli | - |
N-acetyl-D-glucosamine 1-phosphate + CoA | - |
? | |
2.3.1.157 | D-glucosamine 1-phosphate + acetyl-CoA | Escherichia coli JM83 | - |
N-acetyl-D-glucosamine 1-phosphate + CoA | - |
? | |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine | Escherichia coli | amino sugar metabolism | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r | |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine | Escherichia coli | involved in synthesis of peptidoglycan and lipopolysaccharide | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r | |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine | Escherichia coli JM83 | amino sugar metabolism | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.157 | Bacillus subtilis | - |
- |
- |
2.3.1.157 | Escherichia coli | - |
JM83 | - |
2.3.1.157 | Escherichia coli JM83 | - |
JM83 | - |
2.7.7.23 | Escherichia coli | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.3.1.157 | GlmU gene product, bifunctional enzyme with glucosamine-1-phosphate acetyltransferase and uridyltransferase activity | Escherichia coli |
2.7.7.23 | - |
Escherichia coli |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
2.3.1.157 | 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 |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.3.1.157 | 2.2 | - |
GlcN-1-P acetyltransferase activity | Escherichia coli |
2.3.1.157 | 15.1 | - |
GlcNAc-1-P uridyltransferase activity | Escherichia coli |
2.7.7.23 | 15.1 | - |
purified enzyme, pH 8.2, 37°C | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.157 | D-glucosamine 1-phosphate + acetyl-CoA | - |
Bacillus subtilis | N-acetyl-D-glucosamine 1-phosphate + CoA | - |
? | |
2.3.1.157 | D-glucosamine 1-phosphate + acetyl-CoA | - |
Escherichia coli | N-acetyl-D-glucosamine 1-phosphate + CoA | - |
? | |
2.3.1.157 | D-glucosamine 1-phosphate + acetyl-CoA | - |
Escherichia coli JM83 | N-acetyl-D-glucosamine 1-phosphate + CoA | - |
? | |
2.3.1.157 | N-acetyl-D-glucosamine 1-phosphate + UTP | - |
Bacillus subtilis | UDP-N-acetylglucosamine + ? | - |
? | |
2.3.1.157 | 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 | |
2.3.1.157 | 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 | |
2.3.1.157 | UDP-N-acetyl-alpha-D-glucosamine + H2O | - |
Escherichia coli | N-acetyl-D-glucosamine 1-phosphate + UMP | - |
r | |
2.3.1.157 | UDP-N-acetyl-alpha-D-glucosamine + H2O | - |
Escherichia coli JM83 | N-acetyl-D-glucosamine 1-phosphate + UMP | - |
r | |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine | - |
Escherichia coli | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r | |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine | amino sugar metabolism | Escherichia coli | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r | |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine | involved in synthesis of peptidoglycan and lipopolysaccharide | Escherichia coli | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r | |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine | - |
Escherichia coli JM83 | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r | |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine | amino sugar metabolism | Escherichia coli JM83 | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.3.1.157 | trimer | 2 * 49000 or 3 * 49000, dimer or trimer of identical subunits, gel filtration | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.1.157 | GlmU enzyme | - |
Escherichia coli |
2.3.1.157 | GlmU uridyltransferase | - |
Escherichia coli |
2.3.1.157 | UDP-GlcNAc pyrophosphorylase | - |
Escherichia coli |
2.7.7.23 | More | acetyltransferase 5 times higher than uridyltransferase activity | Escherichia coli |
2.7.7.23 | More | bifunctional enzyme with activity of: glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase | Escherichia coli |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.157 | 12.4 | - |
N-acetyl-D-glucosamine 1-phosphate | GmlU uridyltransferase | Escherichia coli |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.3.1.157 | 8.2 | - |
for both acetyltransferase and uridyltransferase | Escherichia coli |
2.7.7.23 | 8.2 | - |
- |
Escherichia coli |