Literature summary for 2.3.1.157 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.

Search for more literature for 2.3.1.157

Cloned(Commentary)

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

Inhibitors

Inhibitors	Comment	Organism	Structure
1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenylamino]-2-(4-pyridyl)-1-ethanone	-	Escherichia coli
EDTA	-	Escherichia coli
terreic acid	isolated from Aspergillus terreus, inhibits the acetyltransferase activity of Escherichia coli GlmU. The inhibition mode is competitive with acetyl-CoA and uncompetitive with alpha-D-glucosamine 1-phosphate. Terreic acid is cytotoxic against Escherichia coli strain ATCC 25922 and inhibit growth of biofilms. Molecular docking and binding structure, and cytotoxic effects, overview; isolated from Aspergillus terreus, inhibits the acetyltransferase domain. Terreic acid is competitive with acetyl-CoA and uncompetitive with alpha-D-glucosamine 1-phosphate and exhibits concentration-dependent killing of Escherichia coli ATCC 25922 up to 4-times minimum inhibitory concentration and inhibits the growth of biofilms generated by Escherichia coli	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Escherichia coli

Natural Substrates/ Products (Substrates)

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	Escherichia coli ATCC 25922	-	CoA + N-acetyl-alpha-D-glucosamine 1-phosphate	-	?

Organism

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	-

Purification (Commentary)

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

Substrates and Products (Substrate)

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	-	Escherichia coli ATCC 25922	CoA + N-acetyl-alpha-D-glucosamine 1-phosphate	-	?

Synonyms

Synonyms	Comment	Organism
GlmU	-	Escherichia coli
N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase	-	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.6	-	assay at	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
acetyl-CoA	-	Escherichia coli

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
additional information	-	additional information	inhibition modes and kinetics, overview	Escherichia coli
0.04029	-	terreic acid	pH 7.6, 37°C, versus acetyl-CoA	Escherichia coli
0.04194	-	terreic acid	pH 7.6, 37°C, versus alpha-D-glucosamine 1-phosphate	Escherichia coli
0.042	-	terreic acid	pH 7.3, 37°C, substrate alpha-D-glucosamine 1-phosphate	Escherichia coli

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.0442	-	pH 7.3, 37°C	Escherichia coli	terreic acid
0.04424	-	pH 7.6, 37°C	Escherichia coli	terreic acid

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Release 2023.1 (January 2023)