Cloned (Comment) | Organism |
---|---|
gene glmU, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
(E)-N-(2,5-dimethylphenyl)-1-(5-nitrofuran-2-yl)methanimine | specific inhibitor, 93.82% inhibition at 0.1 mM | Escherichia coli | |
(E)-N-(2,5-dimethylphenyl)-1-(5-nitrofuran-2-yl)methanimine | - |
Haemophilus influenzae | |
(E)-N-(2-fluoro-5-nitrophenyl)-1-(5-nitrofuran-2-yl)methanimine | specific inhibitor, 97.47% inhibition at 0.1 mM | Escherichia coli | |
(E)-N-(2-fluoro-5-nitrophenyl)-1-(5-nitrofuran-2-yl)methanimine | - |
Haemophilus influenzae | |
1-butyl-2-[(E)-2-(5-nitrofuran-2-yl)ethenyl]-1H-benzimidazole | unspecific inhibitor, 84.26% inhibition at 0.1 mM | Escherichia coli | |
1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenylamino]-2-(4-pyridyl)-1-ethanone | - |
Escherichia coli | |
3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzenesulfonamide | specific inhibitor, 82.87% inhibition at 0.1 mM | Escherichia coli | |
3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzenesulfonamide | - |
Haemophilus influenzae | |
3-hydrazinylquinoline-2-thiol | 93% inhibition at 0.1 mM, competitive with AcCoA and uncompetitive with alpha-D-glucosamine 1-phosphate. Antibacterial activity of the compound corelates with GlmU inhibition; specific inhibitor, 92.68% inhibition at 0.1 mM | Escherichia coli | |
3-hydrazinylquinoline-2-thiol | - |
Haemophilus influenzae | |
5,7-dichloro-2-hydrazinylquinolin-8-ol | 98% inhibition at 0.1 mM, competitive with AcCoA and uncompetitive with alpha-D-glucosamine 1-phosphate. Antibacterial activity of the compound corelates with GlmU inhibition; specific inhibitor, 98.25% inhibition at 0.1 mM | Escherichia coli | |
5,7-dichloro-2-hydrazinylquinolin-8-ol | - |
Haemophilus influenzae | |
6-chloro-N-[3-(methylsulfanyl)phenyl]-3-oxo-3,4-dihydro-2H-1,4-benzoxazine-7-sulfonamide | unspecific inhibitor, 68.69% inhibition at 0.1 mM | Escherichia coli | |
additional information | ligand- and structure-guided screening of a compound library for inhibitors selective for the enzyme's acetyltransferase activity, quantitative two- and three-dimensional structure-activity relationship modelling, overview. Analysis of cytotoxicity of the inhibitors | Escherichia coli | |
N-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]-2-(pyridin-4-yl)acetamide | - |
Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + alpha-D-glucosamine 1-phosphate | Escherichia coli | - |
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
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 ATCC 25922 | - |
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
acetyl-CoA + alpha-D-glucosamine 1-phosphate | Haemophilus influenzae ATCC 51907 | - |
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
additional information | Escherichia coli | the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. Acetyltransfer precedes uridyltransfer with both the acetyltransferase and uridyltransferase reactions taking place in two separable active sites in bifunctional GlmU, where the acetyltransferase domain of GlmU does not show homology with its eukaryotic counterpart | ? | - |
? | |
additional information | Haemophilus influenzae | the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. Acetyltransfer precedes uridyltransfer with both the acetyltransferase and uridyltransferase reactions taking place in two separable active sites in bifunctional GlmU, where the acetyltransferase domain of GlmU does not show homology with its eukaryotic counterpart | ? | - |
? | |
additional information | Escherichia coli ATCC 25922 | the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. Acetyltransfer precedes uridyltransfer with both the acetyltransferase and uridyltransferase reactions taking place in two separable active sites in bifunctional GlmU, where the acetyltransferase domain of GlmU does not show homology with its eukaryotic counterpart | ? | - |
? | |
additional information | Haemophilus influenzae ATCC 51907 | the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. Acetyltransfer precedes uridyltransfer with both the acetyltransferase and uridyltransferase reactions taking place in two separable active sites in bifunctional GlmU, where the acetyltransferase domain of GlmU does not show homology with its eukaryotic counterpart | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Escherichia coli | P0ACC7 | Escherichia coli K-12 | - |
Escherichia coli ATCC 25922 | - |
- |
- |
Escherichia coli ATCC 25922 | P0ACC7 | Escherichia coli K-12 | - |
Haemophilus influenzae | P43889 | - |
- |
Haemophilus influenzae ATCC 51907 | P43889 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + alpha-D-glucosamine 1-phosphate | - |
Escherichia coli | CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
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 ATCC 25922 | CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
acetyl-CoA + alpha-D-glucosamine 1-phosphate | - |
Haemophilus influenzae ATCC 51907 | CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
additional information | the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. Acetyltransfer precedes uridyltransfer with both the acetyltransferase and uridyltransferase reactions taking place in two separable active sites in bifunctional GlmU, where the acetyltransferase domain of GlmU does not show homology with its eukaryotic counterpart | Escherichia coli | ? | - |
? | |
additional information | the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. Acetyltransfer precedes uridyltransfer with both the acetyltransferase and uridyltransferase reactions taking place in two separable active sites in bifunctional GlmU, where the acetyltransferase domain of GlmU does not show homology with its eukaryotic counterpart | Haemophilus influenzae | ? | - |
? | |
additional information | the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. Acetyltransfer precedes uridyltransfer with both the acetyltransferase and uridyltransferase reactions taking place in two separable active sites in bifunctional GlmU, where the acetyltransferase domain of GlmU does not show homology with its eukaryotic counterpart | Escherichia coli ATCC 25922 | ? | - |
? | |
additional information | the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. Acetyltransfer precedes uridyltransfer with both the acetyltransferase and uridyltransferase reactions taking place in two separable active sites in bifunctional GlmU, where the acetyltransferase domain of GlmU does not show homology with its eukaryotic counterpart | Haemophilus influenzae ATCC 51907 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
GlmU | - |
Escherichia coli |
GlmU | - |
Haemophilus influenzae |
N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase | - |
Escherichia coli |
N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase | - |
Haemophilus influenzae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Escherichia coli |
30 | - |
assay at | Haemophilus influenzae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.6 | - |
assay at | Escherichia coli |
7.6 | - |
assay at | Haemophilus influenzae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
acetyl-CoA | - |
Escherichia coli | |
acetyl-CoA | - |
Haemophilus influenzae |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | inhibition modes and kinetics, overview | Escherichia coli | |
additional information | - |
additional information | inhibition modes and kinetics, overview | Haemophilus influenzae |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.0014 | - |
pH not specified in the publication, temperature not specified in the publication | Escherichia coli | 5,7-dichloro-2-hydrazinylquinolin-8-ol | |
0.0014 | - |
pH 7.6, 30°C, recombinant His6-tagged enzyme | Escherichia coli | 5,7-dichloro-2-hydrazinylquinolin-8-ol | |
0.0038 | - |
pH 7.6, 30°C, recombinant His6-tagged enzyme | Escherichia coli | 3-hydrazinylquinoline-2-thiol | |
0.0041 | - |
pH 7.6, 30°C, recombinant His6-tagged enzyme | Escherichia coli | (E)-N-(2-fluoro-5-nitrophenyl)-1-(5-nitrofuran-2-yl)methanimine | |
0.0211 | - |
pH 7.6, 30°C, recombinant His6-tagged enzyme | Escherichia coli | (E)-N-(2,5-dimethylphenyl)-1-(5-nitrofuran-2-yl)methanimine | |
0.0249 | - |
pH 7.6, 30°C, recombinant His6-tagged enzyme | Escherichia coli | 3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzenesulfonamide | |
0.0485 | - |
pH 7.6, 30°C, recombinant His6-tagged enzyme | Haemophilus influenzae | 3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzenesulfonamide | |
0.0661 | - |
pH 7.6, 30°C, recombinant His6-tagged enzyme | Haemophilus influenzae | (E)-N-(2-fluoro-5-nitrophenyl)-1-(5-nitrofuran-2-yl)methanimine | |
0.0799 | - |
pH 7.6, 30°C, recombinant His6-tagged enzyme | Haemophilus influenzae | 5,7-dichloro-2-hydrazinylquinolin-8-ol | |
0.1 | - |
pH 7.6, 30°C, recombinant His6-tagged enzyme | Haemophilus influenzae | 3-hydrazinylquinoline-2-thiol | |
0.1 | - |
pH 7.6, 30°C, recombinant His6-tagged enzyme | Haemophilus influenzae | (E)-N-(2,5-dimethylphenyl)-1-(5-nitrofuran-2-yl)methanimine | |
0.54 | - |
pH 7.6, 30°C, recombinant His6-tagged enzyme | Escherichia coli | N-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]-2-(pyridin-4-yl)acetamide |