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Literature summary extracted from

  • Sharma, R.; Lambu, M.R.; Jamwal, U.; Rani, C.; Chib, R.; Wazir, P.; Mukherjee, D.; Chaubey, A.; Khan, I.A.
    Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) inhibitory activity of terreic acid isolated from Aspergillus terreus (2016), J. Biomol. Screen., 21, 342-353 .
    View publication on PubMed

Cloned(Commentary)

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.157 1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenylamino]-2-(-4-pyridyl)-1-ethanone commercial inhibitor Escherichia coli
2.3.1.157 1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenylamino]-2-(-4-pyridyl)-1-ethanone commercial inhibitor Haemophilus influenzae
2.3.1.157 terreic acid terreic acid inhibits the glucosamine-1-phosphate-acetyltransferase activity of the bifunctional enzyme. Mode of inhibition studies reveal that terreic acid is competitive with AcCoA and uncompetitive with GlcN-1-phosphate. It also exhibits concentration-dependent killing of Escherichia coli strain ATCC 25922 and inhibits the growth of biofilms generated by Escherichia coli. GlmU acetyltransferase is a molecular target of terreic acid, resulting in its antibacterial activity. Terreic acid is isolated from Aspergillus terreus strain MRCJ-356. Molecular modeling, MIC value Escherichia coli
2.3.1.157 terreic acid terreic acid inhibits the glucosamine-1-phosphate-acetyltransferase activity of the bifunctional enzyme. Mode of inhibition studies reveal that terreic acid is competitive with AcCoA and uncompetitive with GlcN-1-phosphate. It also exhibits concentration-dependent killing of Escherichia coli strain ATCC 25922 and inhibits the growth of biofilms generated by Escherichia coli. GlmU acetyltransferase is a molecular target of terreic acid, resulting in its antibacterial activity. Terreic acid is isolated from Aspergillus terreus strain MRCJ-356. Molecular modeling Haemophilus influenzae
2.7.7.23 1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl) phenylamino]-2-(-4-pyridyl)-1-ethanone commercial inhibitor Escherichia coli
2.7.7.23 additional information terreic acid inhibits the glucosamine-1-phosphate-acetyltransferase activity of the bifunctional enzyme. Mode of inhibition studies reveal that terreic acid is competitive with AcCoA and uncompetitive with GlcN-1-phosphate. It also exhibits concentration-dependent killing of Escherichia coli strain ATCC 25922 and inhibits the growth of biofilms generated by Escherichia coli. GlmU acetyltransferase is a molecular target of terreic acid, resulting in its antibacterial activity. Terreic acid is isolated from Aspergillus terreus strain MRCJ-356. Molecular modeling Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.1.157 Mg2+ required Haemophilus influenzae
2.3.1.157 Mg2+ required Escherichia coli
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 Haemophilus influenzae
-
 CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
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 Escherichia coli ATCC 25922
-
 CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
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 P0ACC7
-
-
2.3.1.157 Escherichia coli ATCC 25922 P0ACC7
-
-
2.3.1.157 Haemophilus influenzae
-
-
-
2.7.7.23 Escherichia coli P0ACC7
-
-
2.7.7.23 Escherichia coli ATCC 25922 P0ACC7
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.157 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Haemophilus influenzae
2.3.1.157 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Escherichia coli
2.7.7.23 recombinant His-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
-
 Haemophilus influenzae CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
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
-
 Escherichia coli ATCC 25922 CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
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
-
 Haemophilus influenzae
2.3.1.157 GlmU
-
 Escherichia coli
2.3.1.157 More bifunctional enzyme, cf. EC 2.7.7.23 Haemophilus influenzae
2.3.1.157 More bifunctional enzyme, cf. EC 2.7.7.23 Escherichia coli
2.3.1.157 N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
-
 Haemophilus influenzae
2.3.1.157 N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
-
 Escherichia coli
2.7.7.23 GlmU
-
 Escherichia coli
2.7.7.23 More bifunctional enzyme, cf. EC 2.3.1.157 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 Haemophilus influenzae
2.3.1.157 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 Haemophilus influenzae
2.3.1.157 7.6
-
 assay at Escherichia coli

Cofactor

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

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.3.1.157 0.04424
-
 pH 7.6, 30°C, recombinant enzyme Escherichia coli terreic acid
2.3.1.157 0.09756
-
 pH 7.6, 30°C Haemophilus influenzae terreic acid

General Information

EC Number General Information Comment Organism
2.3.1.157 metabolism pathway and metabolism of UDP-N-acetylglucosamine in prokaryotes and eukaryotes, overview Haemophilus influenzae
2.3.1.157 metabolism pathway and metabolism of UDP-N-acetylglucosamine in prokaryotes and eukaryotes, overview Escherichia coli
2.7.7.23 metabolism pathway and metabolism of UDP-N-acetylglucosamine in prokaryotes and eukaryotes, overview Escherichia coli