Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Sharma, R.; Rani, C.; Mehra, R.; Nargotra, A.; Chib, R.; Rajput, V.; Kumar, S.; Singh, S.; Sharma, P.; Khan, I.
    Identification and characterization of novel small molecule inhibitors of the acetyltransferase activity of Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) (2015), Appl. Microbiol. Biotechnol., 100, 3071-3085.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.157 gene glmU, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) Escherichia coli
2.7.7.23 gene glmU, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.157 (E)-N-(2,5-dimethylphenyl)-1-(5-nitrofuran-2-yl)methanimine specific inhibitor, 93.82% inhibition at 0.1 mM Escherichia coli
2.3.1.157 (E)-N-(2,5-dimethylphenyl)-1-(5-nitrofuran-2-yl)methanimine
-
 Haemophilus influenzae
2.3.1.157 (E)-N-(2-fluoro-5-nitrophenyl)-1-(5-nitrofuran-2-yl)methanimine specific inhibitor, 97.47% inhibition at 0.1 mM Escherichia coli
2.3.1.157 (E)-N-(2-fluoro-5-nitrophenyl)-1-(5-nitrofuran-2-yl)methanimine
-
 Haemophilus influenzae
2.3.1.157 1-butyl-2-[(E)-2-(5-nitrofuran-2-yl)ethenyl]-1H-benzimidazole unspecific inhibitor, 84.26% inhibition at 0.1 mM Escherichia coli
2.3.1.157 1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenylamino]-2-(4-pyridyl)-1-ethanone
-
 Escherichia coli
2.3.1.157 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
2.3.1.157 3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzenesulfonamide
-
 Haemophilus influenzae
2.3.1.157 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
2.3.1.157 3-hydrazinylquinoline-2-thiol
-
 Haemophilus influenzae
2.3.1.157 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
2.3.1.157 5,7-dichloro-2-hydrazinylquinolin-8-ol
-
 Haemophilus influenzae
2.3.1.157 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
2.3.1.157 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
2.3.1.157 N-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]-2-(pyridin-4-yl)acetamide
-
 Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.23 Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.157 acetyl-CoA + alpha-D-glucosamine 1-phosphate Escherichia coli
-
 CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
2.3.1.157 acetyl-CoA + alpha-D-glucosamine 1-phosphate Haemophilus influenzae
-
 CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
2.3.1.157 acetyl-CoA + alpha-D-glucosamine 1-phosphate Escherichia coli ATCC 25922
-
 CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
2.3.1.157 acetyl-CoA + alpha-D-glucosamine 1-phosphate Haemophilus influenzae ATCC 51907
-
 CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
2.3.1.157 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 ?
-
 ?
2.3.1.157 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 ?
-
 ?
2.3.1.157 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 ?
-
 ?
2.3.1.157 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 ?
-
 ?
2.7.7.23 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 ?
-
 ?
2.7.7.23 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 ?
-
 ?
2.7.7.23 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate Escherichia coli
-
 diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?
2.7.7.23 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate Escherichia coli ATCC 25922
-
 diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.157 Escherichia coli
-
-
-
2.3.1.157 Escherichia coli P0ACC7 Escherichia coli K-12
-
2.3.1.157 Escherichia coli ATCC 25922
-
-
-
2.3.1.157 Escherichia coli ATCC 25922 P0ACC7 Escherichia coli K-12
-
2.3.1.157 Haemophilus influenzae P43889
-
-
2.3.1.157 Haemophilus influenzae ATCC 51907 P43889
-
-
2.7.7.23 Escherichia coli P0ACC7 Escherichia coli K-12
-
2.7.7.23 Escherichia coli ATCC 25922 P0ACC7 Escherichia coli K-12
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.157 recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Escherichia coli
2.7.7.23 recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.157 acetyl-CoA + alpha-D-glucosamine 1-phosphate
-
 Escherichia coli CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
2.3.1.157 acetyl-CoA + alpha-D-glucosamine 1-phosphate
-
 Haemophilus influenzae CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
2.3.1.157 acetyl-CoA + alpha-D-glucosamine 1-phosphate
-
 Escherichia coli ATCC 25922 CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
2.3.1.157 acetyl-CoA + alpha-D-glucosamine 1-phosphate
-
 Haemophilus influenzae ATCC 51907 CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
2.3.1.157 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 ?
-
 ?
2.3.1.157 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 ?
-
 ?
2.3.1.157 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 ?
-
 ?
2.3.1.157 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 ?
-
 ?
2.7.7.23 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 ?
-
 ?
2.7.7.23 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 ?
-
 ?
2.7.7.23 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 Escherichia coli diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?
2.7.7.23 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 Escherichia coli ATCC 25922 diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.157 GlmU
-
 Escherichia coli
2.3.1.157 GlmU
-
 Haemophilus influenzae
2.3.1.157 N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
-
 Escherichia coli
2.3.1.157 N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
-
 Haemophilus influenzae
2.7.7.23 GlmU
-
 Escherichia coli
2.7.7.23 N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.157 30
-
 assay at Escherichia coli
2.3.1.157 30
-
 assay at Haemophilus influenzae
2.7.7.23 30
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.157 7.6
-
 assay at Escherichia coli
2.3.1.157 7.6
-
 assay at Haemophilus influenzae
2.7.7.23 7.6
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.157 acetyl-CoA
-
 Escherichia coli
2.3.1.157 acetyl-CoA
-
 Haemophilus influenzae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.3.1.157 additional information
-
 additional information inhibition modes and kinetics, overview Escherichia coli
2.3.1.157 additional information
-
 additional information inhibition modes and kinetics, overview Haemophilus influenzae

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.3.1.157 0.0014
-
 pH not specified in the publication, temperature not specified in the publication Escherichia coli 5,7-dichloro-2-hydrazinylquinolin-8-ol
2.3.1.157 0.0014
-
 pH 7.6, 30°C, recombinant His6-tagged enzyme Escherichia coli 5,7-dichloro-2-hydrazinylquinolin-8-ol
2.3.1.157 0.0038
-
 pH 7.6, 30°C, recombinant His6-tagged enzyme Escherichia coli 3-hydrazinylquinoline-2-thiol
2.3.1.157 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
2.3.1.157 0.0211
-
 pH 7.6, 30°C, recombinant His6-tagged enzyme Escherichia coli (E)-N-(2,5-dimethylphenyl)-1-(5-nitrofuran-2-yl)methanimine
2.3.1.157 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
2.3.1.157 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
2.3.1.157 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
2.3.1.157 0.0799
-
 pH 7.6, 30°C, recombinant His6-tagged enzyme Haemophilus influenzae 5,7-dichloro-2-hydrazinylquinolin-8-ol
2.3.1.157 0.1
-
 pH 7.6, 30°C, recombinant His6-tagged enzyme Haemophilus influenzae 3-hydrazinylquinoline-2-thiol
2.3.1.157 0.1
-
 pH 7.6, 30°C, recombinant His6-tagged enzyme Haemophilus influenzae (E)-N-(2,5-dimethylphenyl)-1-(5-nitrofuran-2-yl)methanimine
2.3.1.157 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

General Information

EC Number General Information Comment Organism
2.7.7.23 physiological function the product of the GlmU catalyzed reactions, UDP-N-acetylglucosamine, is a significant precursor for the peptidoglycan and LPS biosynthesis in Gram-positive and Gram-negative bacteria, respectively Escherichia coli