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acetoacetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetoacetyl-alpha-D-glucosamine 1-phosphate
acetyl-CoA + alpha-D-galactosamine 1-phosphate
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetylglucosamine + ?
n-propionyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-propionyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
propionyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-propionyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
succinyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-succinyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + H2O
N-acetyl-D-glucosamine 1-phosphate + UMP
UDP-N-acetyl-d-glucosamine + diphosphate
N-acetyl-alpha-D-glucosamine 1-phosphate + UTP
additional information
?
-
acetoacetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetoacetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetoacetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetoacetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-galactosamine 1-phosphate
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-galactosamine 1-phosphate
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-galactosamine 1-phosphate
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
r
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
uncommon mode of acetyl-CoA binding in GlmUMtb in the U conformation, which is distinct from the L conformation seen in the available non-mycobacterial GlmU structures. Higly conserved Trp460 is critical for acetyl-CoA binding
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
the enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
the enzyme utilizes ternary complex formation to transfer an acetyl from acetyl-coenzyme A to glucosamine 1-phosphate to form N-acetylglucosamine 1-phosphate. Steady-state kinetic studies and equilibrium binding experiments indicate that GlmU follows a steady-state ordered kinetic mechanism, with acetyl-coenzyme A binding first, which triggers a conformational change in GlmU, followed by glucosamine 1-phosphate binding. Coenzyme A is the last product to dissociate
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
the enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
the enzyme utilizes ternary complex formation to transfer an acetyl from acetyl-coenzyme A to glucosamine 1-phosphate to form N-acetylglucosamine 1-phosphate. Steady-state kinetic studies and equilibrium binding experiments indicate that GlmU follows a steady-state ordered kinetic mechanism, with acetyl-coenzyme A binding first, which triggers a conformational change in GlmU, followed by glucosamine 1-phosphate binding. Coenzyme A is the last product to dissociate
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
because the ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
no activity with alpha-D-glucosamine 6-phosphate. The multifunctional enzyme is also active with acetyl-CoA + alpha-D-galactosamine 1-phosphate (galactosamine-1-phosphate N-acetyltransferase), UTP + N-acetylglucosamine 1-phosphate (EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase) and UTP + N-acetyl-alpha-D-galactosamine 1-phosphate (EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase)
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
because the ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
no activity with alpha-D-glucosamine 6-phosphate. The multifunctional enzyme is also active with acetyl-CoA + alpha-D-galactosamine 1-phosphate (galactosamine-1-phosphate N-acetyltransferase), UTP + N-acetylglucosamine 1-phosphate (EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase) and UTP + N-acetyl-alpha-D-galactosamine 1-phosphate (EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase)
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
the bifunctional enzyme also possesses the activity of EC 2.7.7.23. The C-terminal domain is responsible for the CoA-dependent acetylation of Glc-1-phosphate to GlcNAc-1-phosphate. The N-terminal domain catalyzes uridyl transfer from UTP to GlcNAc-1-phosphate to form the final products UDP-GlcNAc and pyrophosphate
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
presence of acetyl-coenzyme A has an inhibitory effect on uridyltransferase activity of the bifunctional enzyme
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
presence of acetyl-coenzyme A has an inhibitory effect on uridyltransferase activity of the bifunctional enzyme
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine, which is an essential precursor in bacterial cell wall biosynthesis
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine, which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathway
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
a mechanism is proposed in which the activation energy of the double negatively charged phosphorane transition state is lowered by charge compensation of Mg2+ and the side-chain of Lys22
-
-
?
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetylglucosamine + ?
-
-
-
-
?
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetylglucosamine + ?
-
glmU gene product, bifunctional enzyme catalyzing 2 subsequent steps in the pathway for UDP-GlcNAc synthesis
-
-
r
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetylglucosamine + ?
-
glmU gene product, bifunctional enzyme catalyzing 2 subsequent steps in the pathway for UDP-GlcNAc synthesis
-
-
r
UDP-N-acetyl-alpha-D-glucosamine + H2O
N-acetyl-D-glucosamine 1-phosphate + UMP
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine + H2O
N-acetyl-D-glucosamine 1-phosphate + UMP
-
-
-
-
r
UDP-N-acetyl-d-glucosamine + diphosphate
N-acetyl-alpha-D-glucosamine 1-phosphate + UTP
-
-
-
r
UDP-N-acetyl-d-glucosamine + diphosphate
N-acetyl-alpha-D-glucosamine 1-phosphate + UTP
-
-
-
r
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
GlmU also catalyzes the reaction of the N-acetylglucosamine-1-phosphate uridyltransferase, EC 2.7.7.23, catalyzing the synthesis of UDP-GlcNAc from GlcNAc-1-phosphate and UTP
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-
?
additional information
?
-
-
GlmU is a bifunctional enzyme converting alpha-D-glucosamine 1-phosphate to N-acetyl-alpha-D-glucosamine 1-phosphate and then catalyzing the formation of UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate and uridine triphosphate
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-
?
additional information
?
-
-
N-acetyl-glucosamine-1-phosphate uridyltransferase, GlmU, a bifunctional enzyme that catalyzes two key reactions: acetyltransfer and uridyltransfer at two independent domains, overview
-
-
?
additional information
?
-
N-acetyl-glucosamine-1-phosphate uridyltransferase, GlmU, a bifunctional enzyme that catalyzes two key reactions: acetyltransfer and uridyltransfer at two independent domains, overview
-
-
?
additional information
?
-
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase, the enzyme catalyzes the two reactions, acetyl transfer and uridyl transfer, at two independent domains, regulation, overview
-
-
?
additional information
?
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase, the enzyme catalyzes the two reactions, acetyl transfer and uridyl transfer, at two independent domains, regulation, overview
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-
?
additional information
?
-
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively
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-
?
additional information
?
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively
-
-
?
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. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively
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?
additional information
?
-
-
coupled assay method: coupling of the two enzyme reactions via N-acetyl-alpha-D-glucosamine 1-phosphate for determination of the acetyl transferase activity of the enzyme. Substrate recognition and catalytic mechanism for acetyl transfer, overview
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-
?
additional information
?
-
coupled assay method: coupling of the two enzyme reactions via N-acetyl-alpha-D-glucosamine 1-phosphate for determination of the acetyl transferase activity of the enzyme. Substrate recognition and catalytic mechanism for acetyl transfer, overview
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?
additional information
?
-
the recombinant enzyme binds to human interleukin-8, interaction analysis with human neutrophils, overview
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-
?
additional information
?
-
-
the recombinant enzyme binds to human interleukin-8, interaction analysis with human neutrophils, overview
-
-
?
additional information
?
-
GlmU follows a steady-state ordered kinetic mechanism, with acetyl-coenzyme A binding first, which triggers a conformational change in GlmU, followed by glucosamine 1-phosphate binding. Coenzyme A is the last product to dissociate
-
-
-
additional information
?
-
-
GlmU follows a steady-state ordered kinetic mechanism, with acetyl-coenzyme A binding first, which triggers a conformational change in GlmU, followed by glucosamine 1-phosphate binding. Coenzyme A is the last product to dissociate
-
-
-
additional information
?
-
GlmU follows a steady-state ordered kinetic mechanism, with acetyl-coenzyme A binding first, which triggers a conformational change in GlmU, followed by glucosamine 1-phosphate binding. Coenzyme A is the last product to dissociate
-
-
-
additional information
?
-
the recombinant enzyme binds to human interleukin-8, interaction analysis with human neutrophils, overview
-
-
?
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. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively
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-
?
additional information
?
-
the recombinant enzyme binds to human interleukin-8, interaction analysis with human neutrophils, overview
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-
?
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. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively
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additional information
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N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively
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additional information
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the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity. The ST0452 protein can catalyze the acetylation of both GlcN-1-P and GalN-1-P, while GalN-1-P AcTase activity is not detected in bacterial enzymes
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additional information
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the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity. The ST0452 protein can catalyze the acetylation of both GlcN-1-P and GalN-1-P, while GalN-1-P AcTase activity is not detected in bacterial enzymes
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additional information
?
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the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity. The ST0452 protein can catalyze the acetylation of both GlcN-1-P and GalN-1-P, while GalN-1-P AcTase activity is not detected in bacterial enzymes
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additional information
?
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the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity. The ST0452 protein can catalyze the acetylation of both GlcN-1-P and GalN-1-P, while GalN-1-P AcTase activity is not detected in bacterial enzymes
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
acetyl-CoA + alpha-D-galactosamine 1-phosphate
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
additional information
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acetyl-CoA + alpha-D-galactosamine 1-phosphate
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
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acetyl-CoA + alpha-D-galactosamine 1-phosphate
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
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?
acetyl-CoA + alpha-D-galactosamine 1-phosphate
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
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acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
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acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
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acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
r
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
the enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan
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acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
the enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan
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acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
because the ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
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acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
because the ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
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?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
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?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine
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D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
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-
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?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
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?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine, which is an essential precursor in bacterial cell wall biosynthesis
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?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine, which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathway
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additional information
?
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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
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?
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
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additional information
?
-
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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
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?
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
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?
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
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?
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
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additional information
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GlmU also catalyzes the reaction of the N-acetylglucosamine-1-phosphate uridyltransferase, EC 2.7.7.23, catalyzing the synthesis of UDP-GlcNAc from GlcNAc-1-phosphate and UTP
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additional information
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GlmU is a bifunctional enzyme converting alpha-D-glucosamine 1-phosphate to N-acetyl-alpha-D-glucosamine 1-phosphate and then catalyzing the formation of UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate and uridine triphosphate
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additional information
?
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N-acetyl-glucosamine-1-phosphate uridyltransferase, GlmU, a bifunctional enzyme that catalyzes two key reactions: acetyltransfer and uridyltransfer at two independent domains, overview
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additional information
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N-acetyl-glucosamine-1-phosphate uridyltransferase, GlmU, a bifunctional enzyme that catalyzes two key reactions: acetyltransfer and uridyltransfer at two independent domains, overview
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additional information
?
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N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase, the enzyme catalyzes the two reactions, acetyl transfer and uridyl transfer, at two independent domains, regulation, overview
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additional information
?
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N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase, the enzyme catalyzes the two reactions, acetyl transfer and uridyl transfer, at two independent domains, regulation, overview
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additional information
?
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N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively
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?
additional information
?
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N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively
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?
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. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively
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?
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. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively
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?
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. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively
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?
additional information
?
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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(1R,2R)-2-[[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
(1R,2R)-2-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-4-hydroxy-2-methoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
(2E)-4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobut-2-enoic acid
(2E)-4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobut-2-enoic acid
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(4Z)-4-(4-benzyloxybenzylidene)-2-(naphthalen-2-yl)-1,3-oxazol-5(4H)-one
a oxazolidine derivative that specifically inhibits GlmU. Administration to infected mice results in significant decrease in the bacillary load
(5-[(E)-[(2,5-dimethylphenyl)imino]methyl]furan-2-yl)(hydroxy)oxoammonium
(5E)-1-(3,5-dimethylphenyl)-5-(furan-2-ylmethylidene)pyrimidine-2,4,6(1H,3H,5H)-trione
uncompetitive versus acetyl-CoA and alpha-D-glucosamine 1-phosphate, inhibits GlmU enzyme acetyltransferase activity
(5Z)-2-imino-5-[(2E)-3-(5-nitrofuran-2-yl)prop-2-en-1-ylidene]-1,3-thiazolidin-4-one
competitive versus acetyl-CoA, uncompetitive versus alpha-D-glucosamine 1-phosphate, specificly inhibits GlmU acetyltransferase activity and also exhibits whole cell activity against drug susceptible as well as drug resistant Mycobacterium tuberculosis. The compound also exhibits increased anti-tuberculois activity when tested in combination with rifampicin, isoniazid and ethambutol, but is cytotoxxic for the eukaryotic cell line; specific inhibition of acetyltransferase activity, competitive with respect to acetyl-CoA. Compound also exhibits whole cell activity against drug susceptible as well as drug resistant Mycobacterium tuberculosis and increased anti-TB activity when tested in combination with rifampicin, isoniazid and ethambutol. Compound is cytotoxic to eukaryotic cell line
(5Z)-5-(furan-3-ylmethylidene)-1-(4-methoxyphenyl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
uncompetitive versus acetyl-CoA and alpha-D-glucosamine 1-phosphate, inhibits GlmU enzyme acetyltransferase activity
(E)-N-(2,5-dimethylphenyl)-1-(5-nitrofuran-2-yl)methanimine
(E)-N-(2-fluoro-5-nitrophenyl)-1-(5-nitrofuran-2-yl)methanimine
1-(2-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]phenyl)piperidine-4-carboxylic acid
1-butyl-2-[(E)-2-(5-nitrofuran-2-yl)ethenyl]-1H-benzimidazole
unspecific inhibitor, 84.26% inhibition at 0.1 mM
1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenylamino]-2-(-4-pyridyl)-1-ethanone
1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenylamino]-2-(4-pyridyl)-1-ethanone
2'-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]biphenyl-4-carboxylic acid
2-(2-cyanopyridin-4-yl)-N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]acetamide
2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl acetate
2-amino-2,3-dideoxy-3-fluoro-alpha-D-glucopyranosyl phosphate
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2-nitro-5-thiocyanatobenzoic acid
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0.5 mM, 5% residual activity
2-Nitro-5-thiocyanobenzoic acid
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3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzene-1-sulfonamide
3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzenesulfonamide
3-hydrazinylquinoline-2-thiol
3-[(2,4-dimethoxyphenyl)amino]-4-phenylcyclobut-3-ene-1,2-dione
40.0% inhibition at 0.1 mM
4-(4-(benzyloxy)benzylidene)-2-(naphthalen-1-yl)oxazol-5(4H)-one
i.e. Oxa33, syntesis of a specific GlmU inhibitor, molecular docking study, the inhibitor binds to an allosteric site of the uridyltransferase domain., overview. Oxa33 fails to inhibit cell growth even at concentrations as high as 0.150 mM
4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
4-([2,4-dimethoxy-5-[naphthalen-2-yl(phenyl)sulfamoyl]phenyl]amino)-4-oxobutanoic acid
4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
4-([5-[bis(4-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
4-[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]benzoic acid
4-[[(2,6-dimethoxybenzoyl)oxy]imino]cyclohexa-2,5-dien-1-one
competitive versus acetyl-CoA, noncompetitive versus alpha-D-glucosamine 1-phosphate, specificly inhibits GlmU acetyltransferase activity and also exhibits whole cell activity against drug susceptible as well as drug resistant Mycobacterium tuberculosis. The compound also exhibits increased anti-tuberculois activity when tested in combination with rifampicin, isoniazid and ethambutol; specific inhibition of acetyltransferase activity, competitive with respect to acetyl-CoA. Compound also exhibits whole cell activity against drug susceptible as well as drug resistant Mycobacterium tuberculosis and increased anti-TB activity when tested in combination with rifampicin, isoniazid and ethambutol
4-[[2,4-dimethoxy-5-(10H-phenothiazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
4-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
4-[[5-(dibenzo[b,f][1,4]oxazepin-10(11H)-ylsulfonyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
4-[[5-(diphenylsulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
4-[[5-([2-[4-(carboxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
4-[[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
5,5'-dithiobis-(2-nitrobenzoic acid)
-
0.1 mM, 33% residual activity
5,7-dichloro-2-hydrazinylquinolin-8-ol
5-(1,2-oxazol-5-yl)-N-(pyridin-3-ylmethyl)furan-2-sulfonamide
44.7% inhibition at 0.1 mM
6-chloro-N-[3-(methylsulfanyl)phenyl]-3-oxo-3,4-dihydro-2H-1,4-benzoxazine-7-sulfonamide
alpha-D-glucosamine 1-phosphate
-
substrate inhibition, competitive versus N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
Ca2+
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
Co2+
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
D-galactosamine 1-phosphate
-
D-glucosamine 6-phosphate
-
dicumarol
uncompetitively inhibits acetyl CoA and shows mixed-type inhibition for glucosamine-1-phosphate. Dicumarol also exhibits inhibitory effects on several clinically sensitive Mycobacterium tuberculosis strains and drug-resistant strains, with a range of MIC value of 6.25 to more than 100 mg/ml. Dicumarol increases the sensitivity of anti-tuberculosis drugs (isoniazid and rifampicin) when dicumarol is present at a low concentration
ethyl (2-[(Z)-[2-(ethylsulfanyl)-5-oxo-1,3-thiazol-4(5H)-ylidene]methyl]phenoxy)acetate
45.3% inhibition at 0.1 mM
methyl 2-[([[5-(acetylamino)-2,4-dimethoxyphenyl]sulfonyl]amino)methyl]benzoate
Mg2+
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
Mn2+
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
N-(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)acetamide
N-(2,5-dimethoxyphenyl)-N-(phenylsulfonyl)glycine
42.01% inhibition at 0.1 mM
-
N-(3-chlorophenyl)-2-methoxy-5-(2-methyl-1,3-oxazol-5-yl)benzenesulfonamide
406% inhibition at 0.1 mM
N-(5-chloro-2-methoxyphenyl)-N-(phenylsulfonyl)glycine
45.15% inhibition at 0.1 mM
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamothioyl)glycine
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamoyl)glycine
N-acetylglucosamine-1-phosphate
-
acetyltransferase activity inhibited by its reaction product
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-2-(2-fluoropyridin-4-yl)acetamide
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-3-(2H-tetrazol-5-yl)propanamide
N-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]-2-(pyridin-4-yl)acetamide
-
N-[2,4-dimethoxy-5-(10H-phenoxazine-10-sulfonyl)phenyl]-2-(pyridin-4-yl)acetamide
N-[2,4-dimethoxy-5-(phenylsulfamoyl)phenyl]acetamide
N-[2,4-dimethoxy-5-(piperidin-1-ylsulfonyl)phenyl]acetamide
N-[2,4-dimethoxy-5-[(2-methoxybenzyl)sulfamoyl]phenyl]acetamide
N-[2,4-dimethoxy-5-[(2-methyl-2,3-dihydro-1H-indol-1-yl)sulfonyl]phenyl]acetamide
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]-2-(pyridin-4-ylsulfanyl)acetamide
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]benzamide
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]methanesulfonamide
N-[2,4-dimethoxy-5-[(2-methylpyrrolidin-1-yl)sulfonyl]phenyl]acetamide
N-[2,4-dimethoxy-5-[(3-methylphenyl)sulfamoyl]phenyl]acetamide
N-[2,4-dimethoxy-5-[(4-methylphenyl)sulfamoyl]phenyl]acetamide
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
N-[2,4-dimethoxy-5-[phenyl(propan-2-yl)sulfamoyl]phenyl]acetamide
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(2-fluoropyridin-4-yl)acetamide
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(pyridin-4-yl)acetamide
N-[5-(dimethylsulfamoyl)-2,4-dimethoxyphenyl]acetamide
N-[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]acetamide
N-[5-[(1,3-benzodioxol-5-ylmethyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
N-[5-[(2-bromobenzyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
N-[5-[(2-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
N-[5-[(3-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
N-[5-[(4-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
N-[5-[butyl(propan-2-yl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
N-[5-[ethyl(2-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
p-hydroxymercuribenzoate
-
-
UDP-MurNAc
-
1 mM, relative enzyme activity 2%
Zn2+
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]acetic acid
[4-fluoro-3-[(E)-([5-[hydroxy(oxo)azaniumyl]furan-2-yl]methylidene)amino]phenyl](hydroxy)oxoammonium
[5-[(E)-2-(1-butyl-1H-benzimidazol-2-yl)ethenyl]furan-2-yl](hydroxy)oxoammonium
[[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl]sulfanyl]acetic acid
(1R,2R)-2-[[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
-
-
(1R,2R)-2-[[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
-
-
(1R,2R)-2-[[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
-
-
(1R,2R)-2-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
-
-
(1R,2R)-2-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
-
-
(1R,2R)-2-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
-
-
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
-
-
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
-
-
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
-
-
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-4-hydroxy-2-methoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
-
-
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-4-hydroxy-2-methoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
-
-
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-4-hydroxy-2-methoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
-
-
(2E)-4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobut-2-enoic acid
-
-
(2E)-4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobut-2-enoic acid
-
-
(2E)-4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobut-2-enoic acid
-
-
(2E)-4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobut-2-enoic acid
-
-
(5-[(E)-[(2,5-dimethylphenyl)imino]methyl]furan-2-yl)(hydroxy)oxoammonium
-
0.1 mM, 93.82% inhibition, competitive inhibition versus acetyl-CoA, uncompetitive inhibition versus glucose 1-phosphate
(5-[(E)-[(2,5-dimethylphenyl)imino]methyl]furan-2-yl)(hydroxy)oxoammonium
-
-
(E)-N-(2,5-dimethylphenyl)-1-(5-nitrofuran-2-yl)methanimine
specific inhibitor, 93.82% inhibition at 0.1 mM
(E)-N-(2,5-dimethylphenyl)-1-(5-nitrofuran-2-yl)methanimine
-
(E)-N-(2-fluoro-5-nitrophenyl)-1-(5-nitrofuran-2-yl)methanimine
specific inhibitor, 97.47% inhibition at 0.1 mM
(E)-N-(2-fluoro-5-nitrophenyl)-1-(5-nitrofuran-2-yl)methanimine
-
1-(2-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]phenyl)piperidine-4-carboxylic acid
-
-
1-(2-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]phenyl)piperidine-4-carboxylic acid
-
-
1-(2-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]phenyl)piperidine-4-carboxylic acid
-
-
1-(2-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]phenyl)piperidine-4-carboxylic acid
-
-
1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenylamino]-2-(-4-pyridyl)-1-ethanone
commercial inhibitor
1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenylamino]-2-(-4-pyridyl)-1-ethanone
-
commercial inhibitor
1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenylamino]-2-(4-pyridyl)-1-ethanone
-
1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenylamino]-2-(4-pyridyl)-1-ethanone
-
1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenylamino]-2-(4-pyridyl)-1-ethanone
-
2'-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]biphenyl-4-carboxylic acid
-
-
2'-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]biphenyl-4-carboxylic acid
-
-
2'-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]biphenyl-4-carboxylic acid
-
-
2'-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]biphenyl-4-carboxylic acid
-
-
2-(2-cyanopyridin-4-yl)-N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]acetamide
-
-
2-(2-cyanopyridin-4-yl)-N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]acetamide
-
-
2-(2-cyanopyridin-4-yl)-N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]acetamide
-
-
2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl acetate
-
-
2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl acetate
-
-
2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl acetate
-
-
2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl acetate
-
-
3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzene-1-sulfonamide
-
0.1 mM, 82.87% inhibition, competitive inhibition versus acetyl-CoA, uncompetitive inhibition versus glucose 1-phosphate
3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzene-1-sulfonamide
-
-
3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzenesulfonamide
specific inhibitor, 82.87% inhibition at 0.1 mM
3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzenesulfonamide
0.1 mM, 83% inhibition of acetyltransferase activity of GlmU; 82.9% inhibition at 0.1 mM
3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzenesulfonamide
-
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
3-hydrazinylquinoline-2-thiol
-
0.1 mM, 92.68% inhibition, competitive inhibition versus acetyl-CoA, uncompetitive inhibition versus glucose 1-phosphate
3-hydrazinylquinoline-2-thiol
-
3-hydrazinylquinoline-2-thiol
-
-
4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
-
-
4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
-
-
4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
-
-
4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
-
-
4-([2,4-dimethoxy-5-[naphthalen-2-yl(phenyl)sulfamoyl]phenyl]amino)-4-oxobutanoic acid
-
-
4-([2,4-dimethoxy-5-[naphthalen-2-yl(phenyl)sulfamoyl]phenyl]amino)-4-oxobutanoic acid
-
-
4-([2,4-dimethoxy-5-[naphthalen-2-yl(phenyl)sulfamoyl]phenyl]amino)-4-oxobutanoic acid
-
-
4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
-
-
4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
-
-
4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
-
-
4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
-
-
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
-
-
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
-
-
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
-
-
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
-
-
4-([5-[bis(4-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
-
-
4-([5-[bis(4-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
-
-
4-([5-[bis(4-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
-
-
4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
-
-
4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
-
-
4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
-
-
4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
-
-
4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
-
-
4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
-
-
4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
-
-
4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
-
-
4-[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]benzoic acid
-
-
4-[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]benzoic acid
-
-
4-[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]benzoic acid
-
-
4-[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]benzoic acid
-
-
4-[[2,4-dimethoxy-5-(10H-phenothiazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
-
-
4-[[2,4-dimethoxy-5-(10H-phenothiazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
-
-
4-[[2,4-dimethoxy-5-(10H-phenothiazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
-
-
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
-
-
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
-
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
-
-
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
-
substrate inhibition, competitive versus N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
-
-
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
-
-
4-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
-
-
4-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
-
-
4-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
-
-
4-[[5-(dibenzo[b,f][1,4]oxazepin-10(11H)-ylsulfonyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
-
-
4-[[5-(dibenzo[b,f][1,4]oxazepin-10(11H)-ylsulfonyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
-
-
4-[[5-(dibenzo[b,f][1,4]oxazepin-10(11H)-ylsulfonyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
-
-
4-[[5-(diphenylsulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
-
-
4-[[5-(diphenylsulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
-
pH and temperature not specified in the publication
4-[[5-(diphenylsulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
-
pH and temperature not specified in the publication
4-[[5-([2-[4-(carboxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
-
-
4-[[5-([2-[4-(carboxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
-
-
4-[[5-([2-[4-(carboxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
-
-
4-[[5-([2-[4-(carboxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
-
-
4-[[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
-
-
4-[[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
-
-
4-[[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
-
-
4-[[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
-
-
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
5,7-dichloro-2-hydrazinylquinolin-8-ol
-
0.1 mM, 98.25% inhibition, competitive inhibition versus acetyl-CoA, uncompetitive inhibition versus glucose 1-phosphate
5,7-dichloro-2-hydrazinylquinolin-8-ol
-
5,7-dichloro-2-hydrazinylquinolin-8-ol
-
-
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
6-chloro-N-[3-(methylsulfanyl)phenyl]-3-oxo-3,4-dihydro-2H-1,4-benzoxazine-7-sulfonamide
0.1 mM, 69% inhibition of acetyltransferase activity of GlmU. Molecular dynamics simulation and binding site analysis; 68.7% inhibition at 0.1 mM
6-chloro-N-[3-(methylsulfanyl)phenyl]-3-oxo-3,4-dihydro-2H-1,4-benzoxazine-7-sulfonamide
-
0.1 mM, 68.69% inhibition, competitive inhibition versus acetyl-CoA, uncompetitive inhibition versus glucose 1-phosphate
6-chloro-N-[3-(methylsulfanyl)phenyl]-3-oxo-3,4-dihydro-2H-1,4-benzoxazine-7-sulfonamide
-
-
EDTA
-
methyl 2-[([[5-(acetylamino)-2,4-dimethoxyphenyl]sulfonyl]amino)methyl]benzoate
-
-
methyl 2-[([[5-(acetylamino)-2,4-dimethoxyphenyl]sulfonyl]amino)methyl]benzoate
-
-
methyl 2-[([[5-(acetylamino)-2,4-dimethoxyphenyl]sulfonyl]amino)methyl]benzoate
-
-
methyl 2-[([[5-(acetylamino)-2,4-dimethoxyphenyl]sulfonyl]amino)methyl]benzoate
-
-
N-(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)acetamide
-
-
N-(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)acetamide
-
-
N-(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)acetamide
-
-
N-(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)acetamide
-
-
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamothioyl)glycine
-
-
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamothioyl)glycine
-
-
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamothioyl)glycine
-
-
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamothioyl)glycine
-
-
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamoyl)glycine
-
-
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamoyl)glycine
-
-
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamoyl)glycine
-
-
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamoyl)glycine
-
-
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-2-(2-fluoropyridin-4-yl)acetamide
-
-
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-2-(2-fluoropyridin-4-yl)acetamide
-
-
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-2-(2-fluoropyridin-4-yl)acetamide
-
-
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-3-(2H-tetrazol-5-yl)propanamide
-
-
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-3-(2H-tetrazol-5-yl)propanamide
-
-
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-3-(2H-tetrazol-5-yl)propanamide
-
-
N-[2,4-dimethoxy-5-(10H-phenoxazine-10-sulfonyl)phenyl]-2-(pyridin-4-yl)acetamide
-
-
N-[2,4-dimethoxy-5-(10H-phenoxazine-10-sulfonyl)phenyl]-2-(pyridin-4-yl)acetamide
-
-
N-[2,4-dimethoxy-5-(phenylsulfamoyl)phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-(phenylsulfamoyl)phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-(phenylsulfamoyl)phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-(phenylsulfamoyl)phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-(piperidin-1-ylsulfonyl)phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-(piperidin-1-ylsulfonyl)phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-(piperidin-1-ylsulfonyl)phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-(piperidin-1-ylsulfonyl)phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(2-methoxybenzyl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(2-methoxybenzyl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(2-methoxybenzyl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(2-methoxybenzyl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(2-methyl-2,3-dihydro-1H-indol-1-yl)sulfonyl]phenyl]acetamide
-
the inhibitor binds at the C-terminal domain of GlmU engaging the A, B and C subunits of the trimer
N-[2,4-dimethoxy-5-[(2-methyl-2,3-dihydro-1H-indol-1-yl)sulfonyl]phenyl]acetamide
-
the inhibitor binds at the C-terminal domain of GlmU engaging the A, B and C subunits of the trimer
N-[2,4-dimethoxy-5-[(2-methyl-2,3-dihydro-1H-indol-1-yl)sulfonyl]phenyl]acetamide
-
the inhibitor binds at the C-terminal domain of GlmU engaging the A, B and C subunits of the trimer
N-[2,4-dimethoxy-5-[(2-methyl-2,3-dihydro-1H-indol-1-yl)sulfonyl]phenyl]acetamide
-
the inhibitor binds at the C-terminal domain of GlmU engaging the A, B and C subunits of the trimer
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]-2-(pyridin-4-ylsulfanyl)acetamide
-
-
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]-2-(pyridin-4-ylsulfanyl)acetamide
-
-
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]-2-(pyridin-4-ylsulfanyl)acetamide
-
-
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]-2-(pyridin-4-ylsulfanyl)acetamide
-
-
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]benzamide
-
-
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]benzamide
-
-
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]benzamide
-
-
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]benzamide
-
-
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]methanesulfonamide
-
-
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]methanesulfonamide
-
-
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]methanesulfonamide
-
-
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]methanesulfonamide
-
-
N-[2,4-dimethoxy-5-[(2-methylpyrrolidin-1-yl)sulfonyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(2-methylpyrrolidin-1-yl)sulfonyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(2-methylpyrrolidin-1-yl)sulfonyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(2-methylpyrrolidin-1-yl)sulfonyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(3-methylphenyl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(3-methylphenyl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(3-methylphenyl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(3-methylphenyl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(4-methylphenyl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(4-methylphenyl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(4-methylphenyl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(4-methylphenyl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[phenyl(propan-2-yl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[phenyl(propan-2-yl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[phenyl(propan-2-yl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[phenyl(propan-2-yl)sulfamoyl]phenyl]acetamide
-
-
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(2-fluoropyridin-4-yl)acetamide
-
-
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(2-fluoropyridin-4-yl)acetamide
-
-
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(2-fluoropyridin-4-yl)acetamide
-
-
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(pyridin-4-yl)acetamide
-
-
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(pyridin-4-yl)acetamide
-
-
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(pyridin-4-yl)acetamide
-
-
N-[5-(dimethylsulfamoyl)-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-(dimethylsulfamoyl)-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-(dimethylsulfamoyl)-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-(dimethylsulfamoyl)-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(1,3-benzodioxol-5-ylmethyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(1,3-benzodioxol-5-ylmethyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(1,3-benzodioxol-5-ylmethyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(1,3-benzodioxol-5-ylmethyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(2-bromobenzyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(2-bromobenzyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(2-bromobenzyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(2-bromobenzyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(2-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(2-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(2-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(2-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(3-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(3-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(3-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(3-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(4-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(4-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(4-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(4-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[butyl(propan-2-yl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[butyl(propan-2-yl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[butyl(propan-2-yl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[butyl(propan-2-yl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[ethyl(2-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[ethyl(2-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[ethyl(2-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[ethyl(2-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
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
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
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
[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]acetic acid
-
-
[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]acetic acid
-
-
[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]acetic acid
-
-
[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]acetic acid
-
-
[4-fluoro-3-[(E)-([5-[hydroxy(oxo)azaniumyl]furan-2-yl]methylidene)amino]phenyl](hydroxy)oxoammonium
-
0.1 mM, 97.47% inhibition, competitive inhibition versus acetyl-CoA, uncompetitive inhibition versus glucose 1-phosphate
[4-fluoro-3-[(E)-([5-[hydroxy(oxo)azaniumyl]furan-2-yl]methylidene)amino]phenyl](hydroxy)oxoammonium
-
-
[5-[(E)-2-(1-butyl-1H-benzimidazol-2-yl)ethenyl]furan-2-yl](hydroxy)oxoammonium
-
0.1 mM, 84.26% inhibition, competitive inhibition versus acetyl-CoA, uncompetitive inhibition versus glucose 1-phosphate
[5-[(E)-2-(1-butyl-1H-benzimidazol-2-yl)ethenyl]furan-2-yl](hydroxy)oxoammonium
-
-
[[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl]sulfanyl]acetic acid
-
-
[[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl]sulfanyl]acetic acid
-
-
[[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl]sulfanyl]acetic acid
-
-
[[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl]sulfanyl]acetic acid
-
-
additional information
-
high throughput inhibitor screening for inhibition of the acetyltransferase domain of GlmU by a arylsulfonamide series
-
additional information
-
inhibitor synthesis and inhibition potencies, overview
-
additional information
-
inhibitor design from enzyme structure, analysis of antimicrobial compounds mediating their growth inhibitory effects specifically via GlmU, antimicrobial properties of sulfonamide inhibitors of GlmU acetyl transferase, overview
-
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
-
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
-
additional information
-
ligand- and structure-guided screening of a compound library for inhibitors selective for the enzyme's acetyltransferase activity, molecular docking and quantitative two- and three-dimensional structure-activity relationship modelling,, structure-function analysis, overview
-
additional information
ligand- and structure-guided screening of a compound library for inhibitors selective for the enzyme's acetyltransferase activity, molecular docking and quantitative two- and three-dimensional structure-activity relationship modelling,, structure-function analysis, overview
-
additional information
-
high throughput inhibitor screening for inhibition of the acetyltransferase domain of GlmU by a arylsulfonamide series
-
additional information
-
inhibitor synthesis and inhibition potencies, MIC values, overview
-
additional information
-
inhibitor design from enzyme structure, analysis of antimicrobial compounds mediating their growth inhibitory effects specifically via GlmU, antimicrobial properties of sulfonamide inhibitors of GlmU acetyl transferase, overview
-
additional information
-
inhibitor synthesis, detailed overview. No inhibition of GlmU by methyl 2-amino-2-deoxyl-alpha-D-glucopyranoside 6-phosphate, methyl 2-amino-2-deoxyl-beta-D-glucopyranoside 6-phosphate, and 2-azido-2-deoxy-alpha-D-glucopyranosyl phosphate even at high concentrations
-
additional information
-
modelling of competitive and uncompetitive inhibition of Rxn-1 by substrates/products, overview
-
additional information
-
high-throughput screen identifies small molecule inhibitors targeting acetyltransferase activity of Mycobacterium tuberculosis GlmU, molecular docking studies, overview
-
additional information
high-throughput screen identifies small molecule inhibitors targeting acetyltransferase activity of Mycobacterium tuberculosis GlmU, molecular docking studies, overview
-
additional information
-
high throughput inhibitor screening for inhibition of the acetyltransferase domain of GlmU by a arylsulfonamide series
-
additional information
-
inhibitor design from enzyme structure, analysis of antimicrobial compounds mediating their growth inhibitory effects specifically via GlmU, antimicrobial properties of sulfonamide inhibitors of GlmU acetyl transferase, overview
-
additional information
-
high throughput inhibitor screening for inhibition of the acetyltransferase domain of GlmU by a arylsulfonamide series
-
additional information
-
inhibitor synthesis and inhibition potencies, MIC values, overview; inhibitor synthesis and inhibition potencies, overview
-
additional information
-
inhibitor design from enzyme structure, analysis of antimicrobial compounds mediating their growth inhibitory effects specifically via GlmU, antimicrobial properties of sulfonamide inhibitors of GlmU acetyl transferase, overview
-
additional information
residues Tyr311, Lys337 and Lys340 plus C-terminal 11-residue region of the ST0452 protein enhance its GalN-1-P AcTase activity and suppress its GlcN-1-P AcTase activity, this function might be lost in bacterial enzymes
-
additional information
-
residues Tyr311, Lys337 and Lys340 plus C-terminal 11-residue region of the ST0452 protein enhance its GalN-1-P AcTase activity and suppress its GlcN-1-P AcTase activity, this function might be lost in bacterial enzymes
-
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0.0004 - 0.0059
(1R,2R)-2-[[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
0.00038 - 0.00784
(1R,2R)-2-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
0.00001 - 0.0053
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
0.00003 - 0.0303
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-4-hydroxy-2-methoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
0.0005 - 0.2
(2E)-4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobut-2-enoic acid
0.00001
(2E)-4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobut-2-enoic acid
Escherichia coli
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.099
(4Z)-4-(4-benzyloxybenzylidene)-2-(naphthalen-2-yl)-1,3-oxazol-5(4H)-one
Mycobacterium tuberculosis
30°C, pH not specified in the publication
0.02105 - 0.1
(5-[(E)-[(2,5-dimethylphenyl)imino]methyl]furan-2-yl)(hydroxy)oxoammonium
0.01413 - 0.02212
(5E)-1-(3,5-dimethylphenyl)-5-(furan-2-ylmethylidene)pyrimidine-2,4,6(1H,3H,5H)-trione
0.018 - 0.0425
(5Z)-2-imino-5-[(2E)-3-(5-nitrofuran-2-yl)prop-2-en-1-ylidene]-1,3-thiazolidin-4-one
0.00372 - 0.00614
(5Z)-5-(furan-3-ylmethylidene)-1-(4-methoxyphenyl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
0.0211 - 0.1
(E)-N-(2,5-dimethylphenyl)-1-(5-nitrofuran-2-yl)methanimine
0.0041 - 0.0661
(E)-N-(2-fluoro-5-nitrophenyl)-1-(5-nitrofuran-2-yl)methanimine
0.0005 - 0.05
1-(2-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]phenyl)piperidine-4-carboxylic acid
0.0009 - 0.015
2'-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]biphenyl-4-carboxylic acid
0.00067 - 0.01
2-(2-cyanopyridin-4-yl)-N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]acetamide
0.002 - 0.2
2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl acetate
0.0249 - 0.048
3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzene-1-sulfonamide
0.0249 - 0.0485
3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzenesulfonamide
0.00376 - 0.1
3-hydrazinylquinoline-2-thiol
0.00009 - 0.2
4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
0.00004 - 0.0084
4-([2,4-dimethoxy-5-[naphthalen-2-yl(phenyl)sulfamoyl]phenyl]amino)-4-oxobutanoic acid
0.000058 - 0.2
4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
0.000018 - 0.2
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
0.00004 - 0.048
4-([5-[bis(4-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
0.003 - 0.2
4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
0.00025 - 0.2
4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
0.2
4-[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]benzoic acid
0.0322 - 0.065
4-[[(2,6-dimethoxybenzoyl)oxy]imino]cyclohexa-2,5-dien-1-one
0.00009 - 0.0369
4-[[2,4-dimethoxy-5-(10H-phenothiazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
0.000007 - 0.2
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
0.00005 - 0.0466
4-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
0.00003 - 0.055
4-[[5-(dibenzo[b,f][1,4]oxazepin-10(11H)-ylsulfonyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
0.00004 - 0.0255
4-[[5-(diphenylsulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
0.0004 - 0.01
4-[[5-([2-[4-(carboxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
0.003 - 0.2
4-[[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
0.0014 - 0.0799
5,7-dichloro-2-hydrazinylquinolin-8-ol
1
butanoyl-CoA
Mycobacterium tuberculosis
pH 7.5, 30°C
0.3
CoA
Mycobacterium tuberculosis
pH 7.5, 30°C
1
crotonyl-CoA
Mycobacterium tuberculosis
pH 7.5, 30°C
120
D-galactosamine 1-phosphate
Mycobacterium tuberculosis
pH 7.5, 30°C
10
D-glucosamine 6-phosphate
Mycobacterium tuberculosis
pH 7.5, 30°C
5
D-glucose 1-phosphate
Mycobacterium tuberculosis
pH 7.5, 30°C
0.0137
dicumarol
Mycobacterium tuberculosis
pH 7.5, 37°C
2
isobutanoyl-CoA
Mycobacterium tuberculosis
pH 7.5, 30°C
2
malonyl-CoA
Mycobacterium tuberculosis
pH 7.5, 30°C
0.015 - 0.2
methyl 2-[([[5-(acetylamino)-2,4-dimethoxyphenyl]sulfonyl]amino)methyl]benzoate
0.11 - 0.2
N-(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)acetamide
0.0005 - 0.2
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamothioyl)glycine
0.0005 - 0.2
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamoyl)glycine
0.00052 - 0.009
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-2-(2-fluoropyridin-4-yl)acetamide
0.00043 - 0.0247
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-3-(2H-tetrazol-5-yl)propanamide
0.54
N-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]-2-(pyridin-4-yl)acetamide
Escherichia coli
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.00054
N-[2,4-dimethoxy-5-(10H-phenoxazine-10-sulfonyl)phenyl]-2-(pyridin-4-yl)acetamide
Escherichia coli
-
pH 7.3, 37°C
0.02 - 0.2
N-[2,4-dimethoxy-5-(phenylsulfamoyl)phenyl]acetamide
0.08 - 0.2
N-[2,4-dimethoxy-5-(piperidin-1-ylsulfonyl)phenyl]acetamide
0.01 - 0.54
N-[2,4-dimethoxy-5-[(2-methoxybenzyl)sulfamoyl]phenyl]acetamide
0.002 - 0.2
N-[2,4-dimethoxy-5-[(2-methyl-2,3-dihydro-1H-indol-1-yl)sulfonyl]phenyl]acetamide
0.001 - 0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]-2-(pyridin-4-ylsulfanyl)acetamide
0.0015 - 0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]benzamide
0.1 - 0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]methanesulfonamide
0.2
N-[2,4-dimethoxy-5-[(2-methylpyrrolidin-1-yl)sulfonyl]phenyl]acetamide
0.017 - 0.2
N-[2,4-dimethoxy-5-[(3-methylphenyl)sulfamoyl]phenyl]acetamide
0.021 - 0.2
N-[2,4-dimethoxy-5-[(4-methylphenyl)sulfamoyl]phenyl]acetamide
0.003 - 0.2
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
0.002 - 0.2
N-[2,4-dimethoxy-5-[phenyl(propan-2-yl)sulfamoyl]phenyl]acetamide
0.00003 - 0.0099
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(2-fluoropyridin-4-yl)acetamide
0.00003 - 0.032
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(pyridin-4-yl)acetamide
0.2
N-[5-(dimethylsulfamoyl)-2,4-dimethoxyphenyl]acetamide
0.04 - 0.2
N-[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]acetamide
0.2
N-[5-[(1,3-benzodioxol-5-ylmethyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
0.004 - 0.2
N-[5-[(2-bromobenzyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
0.005 - 0.2
N-[5-[(2-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
0.015 - 0.2
N-[5-[(3-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
0.025 - 0.2
N-[5-[(4-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
0.13 - 0.2
N-[5-[butyl(propan-2-yl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
0.015 - 0.2
N-[5-[ethyl(2-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
0.0442 - 0.09756
terreic acid
0.0002 - 0.2
[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]acetic acid
0.00405 - 0.066
[4-fluoro-3-[(E)-([5-[hydroxy(oxo)azaniumyl]furan-2-yl]methylidene)amino]phenyl](hydroxy)oxoammonium
0.0001 - 0.2
[[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl]sulfanyl]acetic acid
0.0004
(1R,2R)-2-[[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.00051
(1R,2R)-2-[[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.0059
(1R,2R)-2-[[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.00038
(1R,2R)-2-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.00048
(1R,2R)-2-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.00784
(1R,2R)-2-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.00001
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.00003
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.0053
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.00003
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-4-hydroxy-2-methoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.00006
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-4-hydroxy-2-methoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.0303
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-4-hydroxy-2-methoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0005
(2E)-4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobut-2-enoic acid
Escherichia coli
-
pH 7.35, 22°C
0.002
(2E)-4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobut-2-enoic acid
Haemophilus influenzae
-
pH 7.35, 22°C
0.01
(2E)-4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobut-2-enoic acid
Streptococcus pneumoniae
-
pH 7.35, 22°C
0.2
(2E)-4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobut-2-enoic acid
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.02105
(5-[(E)-[(2,5-dimethylphenyl)imino]methyl]furan-2-yl)(hydroxy)oxoammonium
Escherichia coli
-
pH 7.3, 37°C
0.1
(5-[(E)-[(2,5-dimethylphenyl)imino]methyl]furan-2-yl)(hydroxy)oxoammonium
Haemophilus influenzae
-
pH 7.3, 37°C
0.01413
(5E)-1-(3,5-dimethylphenyl)-5-(furan-2-ylmethylidene)pyrimidine-2,4,6(1H,3H,5H)-trione
Mycobacterium tuberculosis
versus acetyl-CoA, pH 7.5, 37°C, recombinant enzyme
0.02212
(5E)-1-(3,5-dimethylphenyl)-5-(furan-2-ylmethylidene)pyrimidine-2,4,6(1H,3H,5H)-trione
Mycobacterium tuberculosis
versus alpha-D-glucosamine 1-phosphate, pH 7.5, 37°C, recombinant enzyme
0.018
(5Z)-2-imino-5-[(2E)-3-(5-nitrofuran-2-yl)prop-2-en-1-ylidene]-1,3-thiazolidin-4-one
Mycobacterium tuberculosis
pH not specified in the publication, temperature not specified in the publication
0.0318
(5Z)-2-imino-5-[(2E)-3-(5-nitrofuran-2-yl)prop-2-en-1-ylidene]-1,3-thiazolidin-4-one
Mycobacterium tuberculosis
versus acetyl-CoA, pH 7.5, 37°C, recombinant enzyme
0.0425
(5Z)-2-imino-5-[(2E)-3-(5-nitrofuran-2-yl)prop-2-en-1-ylidene]-1,3-thiazolidin-4-one
Mycobacterium tuberculosis
versus alpha-D-glucosamine 1-phosphate, pH 7.5, 37°C, recombinant enzyme
0.00372
(5Z)-5-(furan-3-ylmethylidene)-1-(4-methoxyphenyl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Mycobacterium tuberculosis
versus acetyl-CoA, pH 7.5, 37°C, recombinant enzyme
0.00614
(5Z)-5-(furan-3-ylmethylidene)-1-(4-methoxyphenyl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Mycobacterium tuberculosis
versus alpha-D-glucosamine 1-phosphate, pH 7.5, 37°C, recombinant enzyme
0.0211
(E)-N-(2,5-dimethylphenyl)-1-(5-nitrofuran-2-yl)methanimine
Escherichia coli
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.1
(E)-N-(2,5-dimethylphenyl)-1-(5-nitrofuran-2-yl)methanimine
Haemophilus influenzae
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.0041
(E)-N-(2-fluoro-5-nitrophenyl)-1-(5-nitrofuran-2-yl)methanimine
Escherichia coli
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.0661
(E)-N-(2-fluoro-5-nitrophenyl)-1-(5-nitrofuran-2-yl)methanimine
Haemophilus influenzae
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.0005
1-(2-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]phenyl)piperidine-4-carboxylic acid
Escherichia coli
-
pH 7.35, 22°C
0.001
1-(2-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]phenyl)piperidine-4-carboxylic acid
Haemophilus influenzae
-
pH 7.35, 22°C
0.002
1-(2-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]phenyl)piperidine-4-carboxylic acid
Streptococcus pneumoniae
-
pH 7.35, 22°C
0.05
1-(2-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]phenyl)piperidine-4-carboxylic acid
Staphylococcus aureus
-
pH 7.35, 22°C
0.0009
2'-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]biphenyl-4-carboxylic acid
Escherichia coli
-
pH 7.35, 22°C
0.005
2'-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]biphenyl-4-carboxylic acid
Haemophilus influenzae
-
pH 7.35, 22°C
0.015
2'-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]biphenyl-4-carboxylic acid
Streptococcus pneumoniae
-
pH 7.35, 22°C
0.00067
2-(2-cyanopyridin-4-yl)-N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]acetamide
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.00068
2-(2-cyanopyridin-4-yl)-N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]acetamide
Escherichia coli
-
pH and temperature not specified in the publication
0.01
2-(2-cyanopyridin-4-yl)-N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]acetamide
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.002
2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl acetate
Haemophilus influenzae
-
pH 7.35, 22°C
0.002
2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl acetate
Escherichia coli
-
pH 7.35, 22°C
0.09
2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl acetate
Streptococcus pneumoniae
-
pH 7.35, 22°C
0.2
2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl acetate
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.0249
3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzene-1-sulfonamide
Escherichia coli
-
pH 7.3, 37°C
0.048
3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzene-1-sulfonamide
Haemophilus influenzae
-
pH 7.3, 37°C
0.0249
3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzenesulfonamide
Escherichia coli
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.0485
3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzenesulfonamide
Haemophilus influenzae
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.00376
3-hydrazinylquinoline-2-thiol
Escherichia coli
-
pH 7.3, 37°C
0.0038
3-hydrazinylquinoline-2-thiol
Escherichia coli
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.1
3-hydrazinylquinoline-2-thiol
Haemophilus influenzae
-
pH 7.3, 37°C
0.1
3-hydrazinylquinoline-2-thiol
Haemophilus influenzae
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.00009
4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
Escherichia coli
-
pH 7.35, 22°C
0.0006
4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
Haemophilus influenzae
-
pH 7.35, 22°C
0.02
4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
Streptococcus pneumoniae
-
pH 7.35, 22°C
0.2
4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.00004
4-([2,4-dimethoxy-5-[naphthalen-2-yl(phenyl)sulfamoyl]phenyl]amino)-4-oxobutanoic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.00083
4-([2,4-dimethoxy-5-[naphthalen-2-yl(phenyl)sulfamoyl]phenyl]amino)-4-oxobutanoic acid
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.0084
4-([2,4-dimethoxy-5-[naphthalen-2-yl(phenyl)sulfamoyl]phenyl]amino)-4-oxobutanoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.000058
4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
Escherichia coli
-
pH 7.2, temperature not specified in the publication
0.00028
4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
Haemophilus influenzae
-
pH 7.2, temperature not specified in the publication
0.0047
4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
Streptococcus pneumoniae
-
pH 7.2, temperature not specified in the publication
0.2
4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
Staphylococcus aureus
-
above, pH 7.2, temperature not specified in the publication
0.000018
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Escherichia coli
-
pH 7.2, temperature not specified in the publication
0.00002
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.0004
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.0004
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Haemophilus influenzae
-
pH 7.2, temperature not specified in the publication
0.04
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Streptococcus pneumoniae
-
pH 7.2, temperature not specified in the publication
0.0402
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.2
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Staphylococcus aureus
-
above, pH 7.2, temperature not specified in the publication
0.00004
4-([5-[bis(4-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.00032
4-([5-[bis(4-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.048
4-([5-[bis(4-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.003
4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
Escherichia coli
-
pH 7.35, 22°C
0.005
4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
Haemophilus influenzae
-
pH 7.35, 22°C
0.012
4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
Streptococcus pneumoniae
-
pH 7.35, 22°C
0.2
4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.00025
4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
Escherichia coli
-
pH 7.35, 22°C
0.0005
4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
Haemophilus influenzae
-
pH 7.35, 22°C
0.0005
4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
Streptococcus pneumoniae
-
pH 7.35, 22°C
0.2
4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
4-[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]benzoic acid
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
4-[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]benzoic acid
Haemophilus influenzae
-
above, pH 7.35, 22°C
0.2
4-[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]benzoic acid
Escherichia coli
-
above, pH 7.35, 22°C
0.2
4-[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]benzoic acid
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.0322
4-[[(2,6-dimethoxybenzoyl)oxy]imino]cyclohexa-2,5-dien-1-one
Mycobacterium tuberculosis
versus alpha-D-glucosamine 1-phosphate, pH 7.5, 37°C, recombinant enzyme
0.0533
4-[[(2,6-dimethoxybenzoyl)oxy]imino]cyclohexa-2,5-dien-1-one
Mycobacterium tuberculosis
versus acetyl-CoA, pH 7.5, 37°C, recombinant enzyme
0.065
4-[[(2,6-dimethoxybenzoyl)oxy]imino]cyclohexa-2,5-dien-1-one
Mycobacterium tuberculosis
pH not specified in the publication, temperature not specified in the publication
0.00009
4-[[2,4-dimethoxy-5-(10H-phenothiazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.00037
4-[[2,4-dimethoxy-5-(10H-phenothiazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.0369
4-[[2,4-dimethoxy-5-(10H-phenothiazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.000007
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Escherichia coli
-
pH 7.2, temperature not specified in the publication
0.00001
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.00001
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Escherichia coli
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.00002
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.000023
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Haemophilus influenzae
-
pH 7.2, temperature not specified in the publication
0.0146
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.015
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Streptococcus pneumoniae
-
pH 7.2, temperature not specified in the publication
0.0215
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.2
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Staphylococcus aureus
-
above, pH 7.2, temperature not specified in the publication
0.00005
4-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.00028
4-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.0466
4-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.00003
4-[[5-(dibenzo[b,f][1,4]oxazepin-10(11H)-ylsulfonyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.00008
4-[[5-(dibenzo[b,f][1,4]oxazepin-10(11H)-ylsulfonyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.055
4-[[5-(dibenzo[b,f][1,4]oxazepin-10(11H)-ylsulfonyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.00004
4-[[5-(diphenylsulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.00091
4-[[5-(diphenylsulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.0255
4-[[5-(diphenylsulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0004
4-[[5-([2-[4-(carboxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Escherichia coli
-
pH 7.35, 22°C
0.002
4-[[5-([2-[4-(carboxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Streptococcus pneumoniae
-
pH 7.35, 22°C
0.003
4-[[5-([2-[4-(carboxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Haemophilus influenzae
-
pH 7.35, 22°C
0.01
4-[[5-([2-[4-(carboxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Staphylococcus aureus
-
pH 7.35, 22°C
0.003
4-[[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Escherichia coli
-
pH 7.35, 22°C
0.005
4-[[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Streptococcus pneumoniae
-
pH 7.35, 22°C
0.006
4-[[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Haemophilus influenzae
-
pH 7.35, 22°C
0.2
4-[[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.0014
5,7-dichloro-2-hydrazinylquinolin-8-ol
Escherichia coli
-
pH 7.3, 37°C
0.0014
5,7-dichloro-2-hydrazinylquinolin-8-ol
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.0014
5,7-dichloro-2-hydrazinylquinolin-8-ol
Escherichia coli
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.079
5,7-dichloro-2-hydrazinylquinolin-8-ol
Haemophilus influenzae
-
pH 7.3, 37°C
0.0799
5,7-dichloro-2-hydrazinylquinolin-8-ol
Haemophilus influenzae
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.015
methyl 2-[([[5-(acetylamino)-2,4-dimethoxyphenyl]sulfonyl]amino)methyl]benzoate
Escherichia coli
-
pH 7.35, 22°C
0.055
methyl 2-[([[5-(acetylamino)-2,4-dimethoxyphenyl]sulfonyl]amino)methyl]benzoate
Haemophilus influenzae
-
pH 7.35, 22°C
0.2
methyl 2-[([[5-(acetylamino)-2,4-dimethoxyphenyl]sulfonyl]amino)methyl]benzoate
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
methyl 2-[([[5-(acetylamino)-2,4-dimethoxyphenyl]sulfonyl]amino)methyl]benzoate
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.11
N-(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)acetamide
Streptococcus pneumoniae
-
pH 7.35, 22°C
0.12
N-(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)acetamide
Haemophilus influenzae
-
pH 7.35, 22°C
0.2
N-(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)acetamide
Escherichia coli
-
above, pH 7.35, 22°C
0.0005
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamothioyl)glycine
Escherichia coli
-
pH 7.35, 22°C
0.001
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamothioyl)glycine
Haemophilus influenzae
-
pH 7.35, 22°C
0.03
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamothioyl)glycine
Streptococcus pneumoniae
-
pH 7.35, 22°C
0.2
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamothioyl)glycine
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.0005
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamoyl)glycine
Escherichia coli
-
pH 7.35, 22°C
0.005
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamoyl)glycine
Haemophilus influenzae
-
pH 7.35, 22°C
0.02
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamoyl)glycine
Streptococcus pneumoniae
-
pH 7.35, 22°C
0.2
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamoyl)glycine
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.00052
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-2-(2-fluoropyridin-4-yl)acetamide
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.0008
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-2-(2-fluoropyridin-4-yl)acetamide
Escherichia coli
-
pH and temperature not specified in the publication
0.009
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-2-(2-fluoropyridin-4-yl)acetamide
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.00043
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-3-(2H-tetrazol-5-yl)propanamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0006
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-3-(2H-tetrazol-5-yl)propanamide
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.0247
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-3-(2H-tetrazol-5-yl)propanamide
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.02
N-[2,4-dimethoxy-5-(phenylsulfamoyl)phenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.07
N-[2,4-dimethoxy-5-(phenylsulfamoyl)phenyl]acetamide
Haemophilus influenzae
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-(phenylsulfamoyl)phenyl]acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-(phenylsulfamoyl)phenyl]acetamide
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.08
N-[2,4-dimethoxy-5-(piperidin-1-ylsulfonyl)phenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-(piperidin-1-ylsulfonyl)phenyl]acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-(piperidin-1-ylsulfonyl)phenyl]acetamide
Haemophilus influenzae
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-(piperidin-1-ylsulfonyl)phenyl]acetamide
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.01
N-[2,4-dimethoxy-5-[(2-methoxybenzyl)sulfamoyl]phenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methoxybenzyl)sulfamoyl]phenyl]acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methoxybenzyl)sulfamoyl]phenyl]acetamide
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.54
N-[2,4-dimethoxy-5-[(2-methoxybenzyl)sulfamoyl]phenyl]acetamide
Haemophilus influenzae
-
pH 7.35, 22°C
0.002
N-[2,4-dimethoxy-5-[(2-methyl-2,3-dihydro-1H-indol-1-yl)sulfonyl]phenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.008
N-[2,4-dimethoxy-5-[(2-methyl-2,3-dihydro-1H-indol-1-yl)sulfonyl]phenyl]acetamide
Haemophilus influenzae
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-2,3-dihydro-1H-indol-1-yl)sulfonyl]phenyl]acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-2,3-dihydro-1H-indol-1-yl)sulfonyl]phenyl]acetamide
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.001
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]-2-(pyridin-4-ylsulfanyl)acetamide
Escherichia coli
-
pH 7.35, 22°C
0.006
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]-2-(pyridin-4-ylsulfanyl)acetamide
Haemophilus influenzae
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]-2-(pyridin-4-ylsulfanyl)acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]-2-(pyridin-4-ylsulfanyl)acetamide
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.0015
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.0021
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
Escherichia coli
-
pH 7.2, temperature not specified in the publication
0.003
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
Haemophilus influenzae
-
pH 7.35, 22°C
0.0078
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
Haemophilus influenzae
-
pH 7.2, temperature not specified in the publication
0.055
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
Streptococcus pneumoniae
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
Staphylococcus aureus
-
above, pH 7.2, temperature not specified in the publication
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
Streptococcus pneumoniae
-
above, pH 7.2, temperature not specified in the publication
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]benzamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]benzamide
Haemophilus influenzae
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]benzamide
Escherichia coli
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]benzamide
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.1
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]methanesulfonamide
Escherichia coli
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]methanesulfonamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]methanesulfonamide
Haemophilus influenzae
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]methanesulfonamide
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methylpyrrolidin-1-yl)sulfonyl]phenyl]acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methylpyrrolidin-1-yl)sulfonyl]phenyl]acetamide
Haemophilus influenzae
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methylpyrrolidin-1-yl)sulfonyl]phenyl]acetamide
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methylpyrrolidin-1-yl)sulfonyl]phenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.017
N-[2,4-dimethoxy-5-[(3-methylphenyl)sulfamoyl]phenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.04
N-[2,4-dimethoxy-5-[(3-methylphenyl)sulfamoyl]phenyl]acetamide
Haemophilus influenzae
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(3-methylphenyl)sulfamoyl]phenyl]acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(3-methylphenyl)sulfamoyl]phenyl]acetamide
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.021
N-[2,4-dimethoxy-5-[(4-methylphenyl)sulfamoyl]phenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.047
N-[2,4-dimethoxy-5-[(4-methylphenyl)sulfamoyl]phenyl]acetamide
Haemophilus influenzae
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(4-methylphenyl)sulfamoyl]phenyl]acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(4-methylphenyl)sulfamoyl]phenyl]acetamide
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.003
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.0033
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
Escherichia coli
-
pH 7.2, temperature not specified in the publication
0.006
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
Haemophilus influenzae
-
pH 7.35, 22°C
0.0064
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
Haemophilus influenzae
-
pH 7.2, temperature not specified in the publication
0.2
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
Staphylococcus aureus
-
above, pH 7.2, temperature not specified in the publication
0.2
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
Streptococcus pneumoniae
-
above, pH 7.2, temperature not specified in the publication
0.2
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.002
N-[2,4-dimethoxy-5-[phenyl(propan-2-yl)sulfamoyl]phenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.016
N-[2,4-dimethoxy-5-[phenyl(propan-2-yl)sulfamoyl]phenyl]acetamide
Haemophilus influenzae
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[phenyl(propan-2-yl)sulfamoyl]phenyl]acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[phenyl(propan-2-yl)sulfamoyl]phenyl]acetamide
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.00003
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(2-fluoropyridin-4-yl)acetamide
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.00009
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(2-fluoropyridin-4-yl)acetamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0099
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(2-fluoropyridin-4-yl)acetamide
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.00003
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(pyridin-4-yl)acetamide
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.00006
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(pyridin-4-yl)acetamide
Escherichia coli
-
pH and temperature not specified in the publication
0.032
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(pyridin-4-yl)acetamide
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.2
N-[5-(dimethylsulfamoyl)-2,4-dimethoxyphenyl]acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[5-(dimethylsulfamoyl)-2,4-dimethoxyphenyl]acetamide
Haemophilus influenzae
-
above, pH 7.35, 22°C
0.2
N-[5-(dimethylsulfamoyl)-2,4-dimethoxyphenyl]acetamide
Escherichia coli
-
above, pH 7.35, 22°C
0.2
N-[5-(dimethylsulfamoyl)-2,4-dimethoxyphenyl]acetamide
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.04
N-[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.07
N-[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]acetamide
Streptococcus pneumoniae
-
pH 7.35, 22°C
0.08
N-[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]acetamide
Haemophilus influenzae
-
pH 7.35, 22°C
0.2
N-[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[5-[(1,3-benzodioxol-5-ylmethyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[5-[(1,3-benzodioxol-5-ylmethyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Haemophilus influenzae
-
above, pH 7.35, 22°C
0.2
N-[5-[(1,3-benzodioxol-5-ylmethyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli
-
above, pH 7.35, 22°C
0.2
N-[5-[(1,3-benzodioxol-5-ylmethyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.004
N-[5-[(2-bromobenzyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.02
N-[5-[(2-bromobenzyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Haemophilus influenzae
-
pH 7.35, 22°C
0.2
N-[5-[(2-bromobenzyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[5-[(2-bromobenzyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.005
N-[5-[(2-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.01
N-[5-[(2-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Haemophilus influenzae
-
pH 7.35, 22°C
0.2
N-[5-[(2-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[5-[(2-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.015
N-[5-[(3-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.03
N-[5-[(3-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Haemophilus influenzae
-
pH 7.35, 22°C
0.2
N-[5-[(3-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[5-[(3-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.025
N-[5-[(4-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.06
N-[5-[(4-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Haemophilus influenzae
-
pH 7.35, 22°C
0.2
N-[5-[(4-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[5-[(4-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.13
N-[5-[butyl(propan-2-yl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.2
N-[5-[butyl(propan-2-yl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[5-[butyl(propan-2-yl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Haemophilus influenzae
-
above, pH 7.35, 22°C
0.2
N-[5-[butyl(propan-2-yl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.015
N-[5-[ethyl(2-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.08
N-[5-[ethyl(2-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Haemophilus influenzae
-
pH 7.35, 22°C
0.2
N-[5-[ethyl(2-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
N-[5-[ethyl(2-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
0.0442
terreic acid
Escherichia coli
pH 7.3, 37°C
0.04424
terreic acid
Escherichia coli
pH 7.6, 37°C
0.04424
terreic acid
Escherichia coli
pH 7.6, 30°C, recombinant enzyme
0.09756
terreic acid
Haemophilus influenzae
-
pH 7.6, 30°C
0.0002
[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]acetic acid
Escherichia coli
-
pH 7.35, 22°C
0.0003
[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]acetic acid
Haemophilus influenzae
-
pH 7.35, 22°C
0.2
[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]acetic acid
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.00405
[4-fluoro-3-[(E)-([5-[hydroxy(oxo)azaniumyl]furan-2-yl]methylidene)amino]phenyl](hydroxy)oxoammonium
Escherichia coli
-
pH 7.3, 37°C
0.066
[4-fluoro-3-[(E)-([5-[hydroxy(oxo)azaniumyl]furan-2-yl]methylidene)amino]phenyl](hydroxy)oxoammonium
Haemophilus influenzae
-
pH 7.3, 37°C
0.0001
[[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl]sulfanyl]acetic acid
Escherichia coli
-
pH 7.35, 22°C
0.0002
[[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl]sulfanyl]acetic acid
Haemophilus influenzae
-
pH 7.35, 22°C
0.2
[[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl]sulfanyl]acetic acid
Staphylococcus aureus
-
above, pH 7.35, 22°C
0.2
[[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl]sulfanyl]acetic acid
Streptococcus pneumoniae
-
above, pH 7.35, 22°C
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evolution
N-acetyl-glucosamine-1-phosphate uridyltransferase, GlmU, is exclusive to prokaryotes, conserved both in Gram positive and Gram negative bacteria
evolution
-
the GlmU proteins encoded by Yersinia pestis and Yersinia pseudotuberculosis are identical in amino acid sequence
evolution
-
the GlmU proteins encoded by Yersinia pestis and Yersinia pseudotuberculosis are identical in amino acid sequence
-
malfunction
Deleting the C-terminal tail, i.e. residues 457-495, of GlmUMtb that provides these residues abolishes all acetyltransferase activity
malfunction
GlmUMtb depletion perturbs cell wall structure and affects the bacterial survival in normoxia, overview
malfunction
-
GlmUMtb depletion perturbs cell wall structure and affects the bacterial survival in normoxia, overview
-
malfunction
-
GlmUMtb depletion perturbs cell wall structure and affects the bacterial survival in normoxia, overview
-
metabolism
N-acetyl-glucosamine-1-phosphate uridyltransferase, GlmU, is a bifunctional enzyme involved in bacterial cell wall synthesis
metabolism
the enzymeis involved in the UDP-N-acetylglucosamine synthesis pathway, overview
metabolism
the bifunctional enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan
metabolism
-
the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
metabolism
-
the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
metabolism
the enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan
metabolism
-
pathway and metabolism of UDP-N-acetylglucosamine in prokaryotes and eukaryotes, overview
metabolism
pathway and metabolism of UDP-N-acetylglucosamine in prokaryotes and eukaryotes, overview
metabolism
-
the bifunctional enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan
-
metabolism
-
the enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan
-
metabolism
-
the enzymeis involved in the UDP-N-acetylglucosamine synthesis pathway, overview
-
metabolism
-
the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
-
metabolism
-
pathway and metabolism of UDP-N-acetylglucosamine in prokaryotes and eukaryotes, overview
-
physiological function
-
essentiality of GlmU to mycobacterial survival
physiological function
-
GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
physiological function
-
GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
physiological function
-
GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
physiological function
-
GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
physiological function
-
GlmU is a bifunctional enzyme with acetyltransferase activity in C-terminus, residues 251-495, and uridyltransferase activity in N-terminus, and it is involved in the biosynthesis of glycosyl donor UDP-N-acetylglucosamine
physiological function
GlmU is involved in the biosynthesis of UDP-N-acetylglucosamine-1-phosphate. It is a bifunctional protein with two independent active sites catalyzing acetyl transfer and uridyl transfer reactions on glucosamine-1-phosphate. It synthesizes two key intermediates of cell wall biosynthesis pathways, viz. N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc. The acetyltransferase activity is catalyzed by the C-terminal domain. It is essential for the growth of the organism
physiological function
-
the bifunctional enzyme N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, catalyzes two-step formation of UDP-GlcNAc, an important precursor in bacterial peptidoglycan and lipopolysaccharide biosynthesis, which are important constituents of the cell wall of both Gram-positive and Gram-negative bacteria. The first activity of GlmU, the C-terminal domain (acetyltransferase), catalyzes the formation of N-acetylglucosamine-1-phosphate from glucosamine-1-phosphate using acetyl-CoA as the acetyl donor. The second activity of GlmU, the N-terminal and rate-limiting domain (uridyltransferase), catalyzes the formation of UDP-GlcNAc from GlcNAc-1-phosphate and uridine triphosphate, UTP
physiological function
-
the C- and N-terminal domains of bifunctional enzyme mycobacterial glucosamine 1-phosphate N-acetyltransferase/N-acetylglucosamine-1-phosphate uridyltransferase catalyze acetyltransferase and uridyltransferase (cf. EC 2.7.7.23) activities, respectively, and the final product is involved in peptidoglycan synthesis
physiological function
-
the C-terminal domain of bifunctional GlmU catalyzes the transfer of an acetyl group from acetyl coenzyme A to glucosamine-1-phosphate to produce N-acetylglucosamine-1-phosphate. In the second step, the N-terminal domain of GlmU catalyzes the transfer of uridyl monophosphate from UTP to acetylglucosamine-1-phosphate to produce UDP-GlcNAc and diphosphate
physiological function
-
the C-terminal domain of bifunctional GlmU catalyzes the transfer of an acetyl group from acetyl coenzyme A to glucosamine-1-phosphate to produce N-acetylglucosamine-1-phosphate. In the second step, the N-terminal domain of GlmU catalyzes the transfer of uridyl monophosphate from UTP to acetylglucosamine-1-phosphate to produce UDP-GlcNAc and diphosphate
physiological function
-
the C-terminal domain of bifunctional GlmU catalyzes the transfer of an acetyl group from acetyl coenzyme A to glucosamine-1-phosphate to produce N-acetylglucosamine-1-phosphate. In the second step, the N-terminal domain of GlmU catalyzes the transfer of uridyl monophosphate from UTP to acetylglucosamine-1-phosphate to produce UDP-GlcNAc and diphosphate
physiological function
-
the C-terminal domain of bifunctional GlmU catalyzes the transfer of an acetyl group from acetyl coenzyme A to glucosamine-1-phosphate to produce N-acetylglucosamine-1-phosphate. In the second step, the N-terminal domain of GlmU catalyzes the transfer of uridyl monophosphate from UTP to acetylglucosamine-1-phosphate to produce UDP-GlcNAc and diphosphate
physiological function
because the ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
physiological function
absence of GlmU leads to extensive perturbation of bacterial morphology and substantial reduction in cell wall thickness under normoxic as well as hypoxic conditions. The acetyl- and uridyl-transferase activities of GlmU are independently essential for bacterial survival in vitro, and GlmU is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. Depletion of GlmU from infected murine lungs, four weeks post infection, leads to significant reduction in the bacillary load
physiological function
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme involved in bacterial cell wall synthesis and is exclusive to prokaryotes. The enzyme is regulated by PknB via phosphorylation at Thr418 causing downregulation of acetyltransferase
physiological function
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively. Final product of GlmU catalyzed reaction, uridine-diphospho-N-acetylglucosamine (UDP-GlcNAc), acts as sugar donor providing GlcNAc residues in the synthesis of peptidoglycan and a disaccharide linker (D-N-GlcNAc-1-rhamnose), the key structural components of Mycobacterium tuberculosis cell wall
physiological function
the acetyl- and uridyltransferase activities of GlmUMtb are independently essential for bacterial survival in vitro, and GlmUMtb is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. The administration of Oxa33, a novel oxazolidine derivative that specifically inhibits GlmUMtb, to infected mice results in significant decrease in the bacillary load. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively
physiological function
the archaeal enzyme's high GalN-1-P AcTase activity, which is not detected on the bacterial and eukaryotic similar enzymes, supports the production of the UDP-GalNAc in archaeal cells
physiological function
-
the bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase enzyme GlmU is an essential gene in Yersinia
physiological function
the enzyme is one of the pathogen proteins that bind to human interleukin-8, IL-8. The binding interaction of mycobacterial proteins AtsG, GlmU and SahH with human IL-8 may indicate that these proteins participate in the modulation of the early events of infection with tubercle bacilli and could affect pathogen attachment to target cells. Interleukin-8 belongs to the family of CXC chemokines and functions as a chemoattractant and activator of different subsets of leukocytes
physiological function
-
GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
-
physiological function
-
because the ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
-
physiological function
-
the archaeal enzyme's high GalN-1-P AcTase activity, which is not detected on the bacterial and eukaryotic similar enzymes, supports the production of the UDP-GalNAc in archaeal cells
-
physiological function
-
the enzyme is one of the pathogen proteins that bind to human interleukin-8, IL-8. The binding interaction of mycobacterial proteins AtsG, GlmU and SahH with human IL-8 may indicate that these proteins participate in the modulation of the early events of infection with tubercle bacilli and could affect pathogen attachment to target cells. Interleukin-8 belongs to the family of CXC chemokines and functions as a chemoattractant and activator of different subsets of leukocytes
-
physiological function
-
absence of GlmU leads to extensive perturbation of bacterial morphology and substantial reduction in cell wall thickness under normoxic as well as hypoxic conditions. The acetyl- and uridyl-transferase activities of GlmU are independently essential for bacterial survival in vitro, and GlmU is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. Depletion of GlmU from infected murine lungs, four weeks post infection, leads to significant reduction in the bacillary load
-
physiological function
-
the acetyl- and uridyltransferase activities of GlmUMtb are independently essential for bacterial survival in vitro, and GlmUMtb is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. The administration of Oxa33, a novel oxazolidine derivative that specifically inhibits GlmUMtb, to infected mice results in significant decrease in the bacillary load. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively
-
physiological function
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively. Final product of GlmU catalyzed reaction, uridine-diphospho-N-acetylglucosamine (UDP-GlcNAc), acts as sugar donor providing GlcNAc residues in the synthesis of peptidoglycan and a disaccharide linker (D-N-GlcNAc-1-rhamnose), the key structural components of Mycobacterium tuberculosis cell wall
-
physiological function
-
the enzyme is one of the pathogen proteins that bind to human interleukin-8, IL-8. The binding interaction of mycobacterial proteins AtsG, GlmU and SahH with human IL-8 may indicate that these proteins participate in the modulation of the early events of infection with tubercle bacilli and could affect pathogen attachment to target cells. Interleukin-8 belongs to the family of CXC chemokines and functions as a chemoattractant and activator of different subsets of leukocytes
-
physiological function
-
absence of GlmU leads to extensive perturbation of bacterial morphology and substantial reduction in cell wall thickness under normoxic as well as hypoxic conditions. The acetyl- and uridyl-transferase activities of GlmU are independently essential for bacterial survival in vitro, and GlmU is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. Depletion of GlmU from infected murine lungs, four weeks post infection, leads to significant reduction in the bacillary load
-
physiological function
-
the acetyl- and uridyltransferase activities of GlmUMtb are independently essential for bacterial survival in vitro, and GlmUMtb is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. The administration of Oxa33, a novel oxazolidine derivative that specifically inhibits GlmUMtb, to infected mice results in significant decrease in the bacillary load. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively
-
physiological function
-
the bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase enzyme GlmU is an essential gene in Yersinia
-
physiological function
-
GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
-
physiological function
-
the archaeal enzyme's high GalN-1-P AcTase activity, which is not detected on the bacterial and eukaryotic similar enzymes, supports the production of the UDP-GalNAc in archaeal cells
-
physiological function
-
GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
-
physiological function
-
GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
-
additional information
-
analysis of structures of GlmUMtb bound to substrates of the acetyl transfer reaction
additional information
analysis of structures of GlmUMtb bound to substrates of the acetyl transfer reaction
additional information
the C-terminal tail region of the ST0452 protein might be important for recognition of the multiple substrates for amino-sugar-1-P AcTase activity. The ST0452 protein contains only two Cys residues, it is unlikely that Cys-Cys bonds contribute to its thermostability. Residue Asn331 in the ST0452 protein is essential for the GalN-1-P AcTase activity, but it is much less important and not essential for the GlcN-1-P AcTase activity. The C-terminal residues of the ST0452 protein enhance the turnover rate of its GalN-1-P AcTase catalytic activity and slightly suppress substrate binding. Residue H308 is essential for both amino-sugar-1-P AcTase activities of the ST0452 protein
additional information
-
the C-terminal tail region of the ST0452 protein might be important for recognition of the multiple substrates for amino-sugar-1-P AcTase activity. The ST0452 protein contains only two Cys residues, it is unlikely that Cys-Cys bonds contribute to its thermostability. Residue Asn331 in the ST0452 protein is essential for the GalN-1-P AcTase activity, but it is much less important and not essential for the GlcN-1-P AcTase activity. The C-terminal residues of the ST0452 protein enhance the turnover rate of its GalN-1-P AcTase catalytic activity and slightly suppress substrate binding. Residue H308 is essential for both amino-sugar-1-P AcTase activities of the ST0452 protein
additional information
-
the catalytic mechanism operative in GlmUMtb performs a SN2 reaction, His374 and Asn397 act as catalytic residues by enhancing the nucleophilicity of the attacking amino group of glucosamine 1-phosphate. Ser416 and Trp460, on a short helix, provide important interactions for substrate binding. The enzyme shows an uncommon mode of binding with acetyl-CoA. GlmU from Mycobacterium tuberculosis possesses a unique 30-residue extension at the C-terminus. The adenine base of acetyl-CoA bound to GlmUMtb is buried at the interface of two monomers of the trimer
additional information
the catalytic mechanism operative in GlmUMtb performs a SN2 reaction, His374 and Asn397 act as catalytic residues by enhancing the nucleophilicity of the attacking amino group of glucosamine 1-phosphate. Ser416 and Trp460, on a short helix, provide important interactions for substrate binding. The enzyme shows an uncommon mode of binding with acetyl-CoA. GlmU from Mycobacterium tuberculosis possesses a unique 30-residue extension at the C-terminus. The adenine base of acetyl-CoA bound to GlmUMtb is buried at the interface of two monomers of the trimer
additional information
-
the C-terminal tail region of the ST0452 protein might be important for recognition of the multiple substrates for amino-sugar-1-P AcTase activity. The ST0452 protein contains only two Cys residues, it is unlikely that Cys-Cys bonds contribute to its thermostability. Residue Asn331 in the ST0452 protein is essential for the GalN-1-P AcTase activity, but it is much less important and not essential for the GlcN-1-P AcTase activity. The C-terminal residues of the ST0452 protein enhance the turnover rate of its GalN-1-P AcTase catalytic activity and slightly suppress substrate binding. Residue H308 is essential for both amino-sugar-1-P AcTase activities of the ST0452 protein
-
additional information
-
the C-terminal tail region of the ST0452 protein might be important for recognition of the multiple substrates for amino-sugar-1-P AcTase activity. The ST0452 protein contains only two Cys residues, it is unlikely that Cys-Cys bonds contribute to its thermostability. Residue Asn331 in the ST0452 protein is essential for the GalN-1-P AcTase activity, but it is much less important and not essential for the GlcN-1-P AcTase activity. The C-terminal residues of the ST0452 protein enhance the turnover rate of its GalN-1-P AcTase catalytic activity and slightly suppress substrate binding. Residue H308 is essential for both amino-sugar-1-P AcTase activities of the ST0452 protein
-
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C380A
the acetyltransferase activity of the mutant is 2.6fold higher than that of the wild type enzyme
C380A/C405S
the double mutant has an increased kcat/Km value compared to the wild type enzyme
C405A
the mutant shows a slight increase in activity compared to the wild type enzyme
C405S
the mutant has an increased kcat/Km value compared to the wild type enzyme
V385C/C405S
the double mutant has an increased kcat/Km value compared to the wild type enzyme
C380A
-
the acetyltransferase activity of the mutant is 2.6fold higher than that of the wild type enzyme
-
C380A/C405S
-
the double mutant has an increased kcat/Km value compared to the wild type enzyme
-
C405A
-
the mutant shows a slight increase in activity compared to the wild type enzyme
-
C405S
-
the mutant has an increased kcat/Km value compared to the wild type enzyme
-
V385C/C405S
-
the double mutant has an increased kcat/Km value compared to the wild type enzyme
-
A451R
site-directed mutagenesis, neither the single mutants A451R and R439T nor the double mutant A451R/R439T affect the acetyltransferase activity significantly
A451R/R439T
site-directed mutagenesis, neither the single mutants A451R and R439T nor the double mutant A451R/R439T affect the acetyltransferase activity significantly
E458A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, 86% of wild-type acetyltransferase activity is remaining
K362A
-
site-directed mutagenesis, the enzyme activity of the mutant is abolished by more than 90% of the wild-type acetyltransferase, and the affinity with the two substrates is completely lost
K403A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, 27% of wild-type acetyltransferase activity is remaining
K464A/W460A
site-directed mutagenesis, the mutant shows highly compromised activity compared to the wild-type enzyme
N456A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme, 67% of wild-type acetyltransferase activity is remaining
R439T
site-directed mutagenesis, neither the single mutants A451R and R439T nor the double mutant A451R/R439T affect the acetyltransferase activity significantly
R463A
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
S474A
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
T296A
-
in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU
T308A/T309A/T311A
-
in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU
T324A/T341A/T347A
-
in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU
T365A/T368A/T370A
-
in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU
T376A/T401A/T406A/T407A
-
in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU
T414A/T418A/T425/T432A/T436A
-
in vitro kinase assays show that the mutant protein is not phosphorylated as the wild-type GlmU. These results confine PknB-mediated phosphorylation sites to a smaller region between amino acids 414 and 439 that harbors five threonines
T418S
site-directed mutagenesis, the acetyltransferase activity of the mutant is compromised as compared with GlmUMtb wild-type, the mutant shows 19% acetyltransferase activity and 108.8% of uridinyltransferase activity compared to the wild-type
T486A/T494A
-
in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU
W460A/K64A
site-directed mutagenesis, the mutant shows 7.8% acetyltransferase activity and 104.7% of uridinyltransferase activity compared to the wild-type
Y398A
-
site-directed mutagenesis, the enzyme activity of the mutant is abolished by more than 90% of the wild-type acetyltransferase, and the affinity with the two substrates is completely lost
K337A
site-directed mutagenesis, the mutant enzyme shows slightly decreasing GalN-1-P AcTase activity and slightly increasing GlcN-1-P AcTase activity compared to the wild-type enzyme. The mutant shows 82.6% and 137.7% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively
K377A
specific activity is 137.7% compared to the wild-type enzyme
T80S/Y97N
the mutant enzyme shows 6.5times-higher activity, compared to that of the wild-type ST0452 protein, revealing that these two substituted residues function cooperatively to increase N-acetylglucosamine-1-phosphate uridyltransferase activity
Y103N
mutant enzyme shows increased GlcNAc-1-P UTase activity
Y97A
mutant enzyme exhibits the highest activity of the single-mutant proteins
Y97N
the mutant enzyme exhibits over 4 times higher N-acetylglucosamine-1-phosphate uridyltransferase activity, compared with that of the wild-type ST0452 protein. The three-dimensional structure of the Y97N protein is not changed by this substitution but the interactions with the substrate are slightly modified, which might cause the activity to increase. The crystal structure of the Y97N protein shows that positions 146 (Glu) and 80 (Thr) form interactions with GlcNAc, and an engineering strategy is applied to these residues to increase activity
K340A
-
specific activity is 147.1% compared to the wild-type enzyme
-
T80S/Y97N
-
the mutant enzyme shows 6.5times-higher activity, compared to that of the wild-type ST0452 protein, revealing that these two substituted residues function cooperatively to increase N-acetylglucosamine-1-phosphate uridyltransferase activity
-
Y103N
-
mutant enzyme shows increased GlcNAc-1-P UTase activity
-
Y97A
-
mutant enzyme exhibits the highest activity of the single-mutant proteins
-
Y97N
-
the mutant enzyme exhibits over 4 times higher N-acetylglucosamine-1-phosphate uridyltransferase activity, compared with that of the wild-type ST0452 protein. The three-dimensional structure of the Y97N protein is not changed by this substitution but the interactions with the substrate are slightly modified, which might cause the activity to increase. The crystal structure of the Y97N protein shows that positions 146 (Glu) and 80 (Thr) form interactions with GlcNAc, and an engineering strategy is applied to these residues to increase activity
-
K340A
-
specific activity is 147.1% compared to the wild-type enzyme
-
H374A
-
site-directed mutagenesis, the enzyme activity of the mutant is abolished by more than 90% of the wild-type acetyltransferase, and the affinity with the two substrates is completely lost
H374A
site-directed mutagenesis, the mutant shows highly reduced Vmax in acetyltransfer compared to the wild-type enzyme
H374A
site-directed mutagenesis, the acetyltransferase active site mutant shows 1.7% of acetyltransferase activity and 96.7% of uridinyltransferase activity compared to the wild-type
K464A
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
K464A
site-directed mutagenesis, the mutant still shows acetyltransferase activity, the mutant shows 105.6% acetyltransferase activity and 97.9% of uridinyltransferase activity compared to the wild-type
N397A
site-directed mutagenesis, the mutant shows highly reduced Vmax in acetyltransfer compared to the wild-type enzyme
N397A
site-directed mutagenesis, the acetyltransferase active site mutant shows 5.2% of acetyltransferase activity and 113.6% of uridinyltransferase activity compared to the wild-type
S416A
site-directed mutagenesis, the mutant shows kinetics in acetyltransfer similar to the wild-type enzyme, S416 neither plays a role in catalysis nor in substrate binding
S416A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, 65% of wild-type acetyltransferase activity is remaining
S416A
site-directed mutagenesis, the acetyltransferase active site mutant shows 100.9% of acetyltransferase activity and 96.4% of uridinyltransferase activity compared to the wild-type
T418A
site-directed mutagenesis, T418 is the most abundant phosphorylation site on GlmUMtb, acetyltransferase activity is completely abolishe
T418A
site-directed mutagenesis, the acetyltransferase activity of mutant is severely compromised as compared with GlmUMtb wild-type, the mutant shows 2.4% acetyltransferase activity and 100.4% of uridinyltransferase activity compared to the wild-type
T418E
site-directed mutagenesis, acetyltransferase activity of T418E mutant that mimics a phosphorylated Thr, is severely compromised compared to wild-type GlmUMtb
T418E
site-directed mutagenesis, the acetyltransferase activity of the T418E mutant that mimics a phosphorylated Thr, is severely compromised as compared with GlmUMtb wild-type, the mutant shows 2.2% acetyltransferase activity and 109.2% of uridinyltransferase activity compared to the wild-type
W460A
-
site-directed mutagenesis, the enzyme activity of the mutant is abolished by more than 90% of the wild-type acetyltransferase, and the affinity with the two substrates is completely lost
W460A
site-directed mutagenesis, the mutant shows highly compromised activity compared to the wild-type enzyme
W460A
site-directed mutagenesis, the mutant displays almost complete loss in acetyltransferase activity, the mutant shows 8.4% acetyltransferase activity and 99.8% of uridinyltransferase activity compared to the wild-type
H308A
specific activity is 0.7% compared to the wild-type enzyme
H308A
site-directed mutagenesis, the mutation diminishes both amino-sugar-1-P AcTase activities of the ST0452 protein. The mutant shows 7.7% and 0.7% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively
K340A
specific activity is 147.1% compared to the wild-type enzyme
K340A
site-directed mutagenesis, the mutant enzyme shows moderately decreasing GalN-1-P AcTase activity and moderately increasing GlcN-1-P AcTase activity compared to the wild-type enzyme. The mutant shows 63.3% and 147.1% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively
N331A
specific activity is 46.1% compared to the wild-type enzyme
N331A
site-directed mutagenesis, the mutant enzyme shows highly decreasing GalN-1-P AcTase activity and decreasing GlcN-1-P AcTase activity compared to the wild-type enzyme. The mutant shows 3.1% and 46.1% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively
Y311A
specific activity is 118.4% compared to the wild-type enzyme
Y311A
site-directed mutagenesis, the mutant enzyme shows highly decreasing GalN-1-P AcTase activity and increasing GlcN-1-P AcTase activity compared to the wild-type enzyme. The mutant shows 3.3% and 118.4% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively
H308A
-
specific activity is 0.7% compared to the wild-type enzyme
-
H308A
-
site-directed mutagenesis, the mutation diminishes both amino-sugar-1-P AcTase activities of the ST0452 protein. The mutant shows 7.7% and 0.7% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively
-
H308A
-
specific activity is 0.7% compared to the wild-type enzyme
-
H308A
-
site-directed mutagenesis, the mutation diminishes both amino-sugar-1-P AcTase activities of the ST0452 protein. The mutant shows 7.7% and 0.7% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively
-
C307S
-
site-directed mutagenesis
C307S
-
site-directed mutagenesis
-
additional information
construction of Mycobacterium tuberculosis mutant strains overproducing GlmU allows determination of the contribution of the protein to mycobacterial entry into human neutrophils
additional information
-
construction of Mycobacterium tuberculosis mutant strains overproducing GlmU allows determination of the contribution of the protein to mycobacterial entry into human neutrophils
additional information
-
construction of Mycobacterium tuberculosis mutant strains overproducing GlmU allows determination of the contribution of the protein to mycobacterial entry into human neutrophils
-
additional information
-
construction of Mycobacterium tuberculosis mutant strains overproducing GlmU allows determination of the contribution of the protein to mycobacterial entry into human neutrophils
-
additional information
glucosamine-1-phosphate acetyltransferase activity of C-terminal deletion mutants DC005 and DC011 (deletion of the C-terminal 5 or 11 residues of the ST0452 protein) are respectively, 4.8 and 16.8 times higher than that of the wild-type ST0452 protein. The mutant enzyme DC011 (deletion of the C-terminal 11 residues of the ST0452 protein) shows little thermal stability at 80°C. The C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein. The deletion mutant enzymes DC021, DC031, DC041, DC071 and DC121, are produced in an insoluble form or aggregated immediately after purification. Mutant enzymes DC051 and DC171 can be expressed in a soluble form. Mutant enzyme DC051 becomes completely insoluble after 5 min treatment at 60°C, while mutant enzyme DC171 is insoluble after 5 min treatment at 70 °C
additional information
-
glucosamine-1-phosphate acetyltransferase activity of C-terminal deletion mutants DC005 and DC011 (deletion of the C-terminal 5 or 11 residues of the ST0452 protein) are respectively, 4.8 and 16.8 times higher than that of the wild-type ST0452 protein. The mutant enzyme DC011 (deletion of the C-terminal 11 residues of the ST0452 protein) shows little thermal stability at 80°C. The C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein. The deletion mutant enzymes DC021, DC031, DC041, DC071 and DC121, are produced in an insoluble form or aggregated immediately after purification. Mutant enzymes DC051 and DC171 can be expressed in a soluble form. Mutant enzyme DC051 becomes completely insoluble after 5 min treatment at 60°C, while mutant enzyme DC171 is insoluble after 5 min treatment at 70 °C
additional information
construction of expression vectors encoding a series of ST0452 C-terminal deletion mutants with hexahistidine tags at their C-termini, designated pST0452(DC005)H, pST0452(DC011)H, pST0452(DC021)H, pST0452(DC031)H, pST0452(DC041) H, pST0452(DC051)H, pST0452(DC071)H, pST0452 (DC121)H and pST0452(DC171)H. The deletion mutants retain the same tertiary structures as the wild-type ST0452 protein, but some show an altered thermostability, overview
additional information
-
construction of expression vectors encoding a series of ST0452 C-terminal deletion mutants with hexahistidine tags at their C-termini, designated pST0452(DC005)H, pST0452(DC011)H, pST0452(DC021)H, pST0452(DC031)H, pST0452(DC041) H, pST0452(DC051)H, pST0452(DC071)H, pST0452 (DC121)H and pST0452(DC171)H. The deletion mutants retain the same tertiary structures as the wild-type ST0452 protein, but some show an altered thermostability, overview
additional information
-
glucosamine-1-phosphate acetyltransferase activity of C-terminal deletion mutants DC005 and DC011 (deletion of the C-terminal 5 or 11 residues of the ST0452 protein) are respectively, 4.8 and 16.8 times higher than that of the wild-type ST0452 protein. The mutant enzyme DC011 (deletion of the C-terminal 11 residues of the ST0452 protein) shows little thermal stability at 80°C. The C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein. The deletion mutant enzymes DC021, DC031, DC041, DC071 and DC121, are produced in an insoluble form or aggregated immediately after purification. Mutant enzymes DC051 and DC171 can be expressed in a soluble form. Mutant enzyme DC051 becomes completely insoluble after 5 min treatment at 60°C, while mutant enzyme DC171 is insoluble after 5 min treatment at 70 °C
-
additional information
-
construction of expression vectors encoding a series of ST0452 C-terminal deletion mutants with hexahistidine tags at their C-termini, designated pST0452(DC005)H, pST0452(DC011)H, pST0452(DC021)H, pST0452(DC031)H, pST0452(DC041) H, pST0452(DC051)H, pST0452(DC071)H, pST0452 (DC121)H and pST0452(DC171)H. The deletion mutants retain the same tertiary structures as the wild-type ST0452 protein, but some show an altered thermostability, overview
-
additional information
-
glucosamine-1-phosphate acetyltransferase activity of C-terminal deletion mutants DC005 and DC011 (deletion of the C-terminal 5 or 11 residues of the ST0452 protein) are respectively, 4.8 and 16.8 times higher than that of the wild-type ST0452 protein. The mutant enzyme DC011 (deletion of the C-terminal 11 residues of the ST0452 protein) shows little thermal stability at 80°C. The C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein. The deletion mutant enzymes DC021, DC031, DC041, DC071 and DC121, are produced in an insoluble form or aggregated immediately after purification. Mutant enzymes DC051 and DC171 can be expressed in a soluble form. Mutant enzyme DC051 becomes completely insoluble after 5 min treatment at 60°C, while mutant enzyme DC171 is insoluble after 5 min treatment at 70 °C
-
additional information
-
construction of expression vectors encoding a series of ST0452 C-terminal deletion mutants with hexahistidine tags at their C-termini, designated pST0452(DC005)H, pST0452(DC011)H, pST0452(DC021)H, pST0452(DC031)H, pST0452(DC041) H, pST0452(DC051)H, pST0452(DC071)H, pST0452 (DC121)H and pST0452(DC171)H. The deletion mutants retain the same tertiary structures as the wild-type ST0452 protein, but some show an altered thermostability, overview
-
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Mengin-Lecreulx, D.; van Heijenoort, J.
Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis
J. Bacteriol.
176
5788-5795
1994
Bacillus subtilis, Escherichia coli, Escherichia coli JM83
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Pompeo, F.; Van Heijenoort, J.; Mengin-Lecreulx, D.
Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes
J. Bacteriol.
180
4799-4803
1998
Bacillus subtilis, Escherichia coli, Neisseria gonorrhoeae, Escherichia coli JM83
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Olsen, L.R.; Tian, Y.; Roderick, S.L.
Purification, crystallization and preliminary x-ray data for Escherichia coli GlmU: a bifunctional acetyltransferase/uridyltransferase
Acta Crystallogr. Sect. D
57
296-297
2001
Escherichia coli
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Pompeo, F.; Bourne, Y.; Van Heijenoort, J.; Fassy, F.; Mengin-Lecreulx, D.
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into autonomously functional domains and evidence that trimerization is absolutely required for glucosamine-1-phosphate acetyltransferase activity and cell growth
J. Biol. Chem.
276
3833-3839
2001
Escherichia coli, Escherichia coli JM83
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Sulzenbacher, G.; Gal, L.; Peneff, C.; Fassy, F.; Bourne, Y.
Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture
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276
11844-11851
2001
Streptococcus pneumoniae (Q97R46), Streptococcus pneumoniae
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Olsen, L.R.; Roderick, S.L.
Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites
Biochemistry
40
1913-1921
2001
Escherichia coli (P0ACC7)
brenda
Kostrewa, D.; D'Arcy, A.; Takacs, B.; Kamber, M.
Crystal structures of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, in apo form at 2.33 A resolution and in complex with UDP-N-acetylglucosamine and Mg(2+) at 1.96 A resolution
J. Mol. Biol.
305
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2001
Streptococcus pneumoniae (Q97R46), Streptococcus pneumoniae
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Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products
Protein Sci.
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Escherichia coli
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Expression, essentiality, and a microtiter plate assay for mycobacterial GlmU, the bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase
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Mycobacterium tuberculosis (P9WMN3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WMN3), Mycobacterium tuberculosis H37Rv
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Zhang, Z.; Bulloch, E.M.; Bunker, R.D.; Baker, E.N.; Squire, C.J.
Structure and function of GlmU from Mycobacterium tuberculosis
Acta Crystallogr. Sect. D
65
275-283
2009
Mycobacterium tuberculosis (P9WMN3), Mycobacterium tuberculosis H37Rv (P9WMN3)
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Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group
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2009
Mycobacterium tuberculosis (P9WMN3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WMN3)
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PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-phosphate uridyltransferase, modulates its acetyltransferase activity
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Mycobacterium tuberculosis
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Structure of a small-molecule inhibitor complexed with GlmU from Haemophilus influenzae reveals an allosteric binding site
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Inhibitors of acetyltransferase domain of N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU). Part 1: Hit to lead evaluation of a novel arylsulfonamide series
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