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Information on EC 2.3.1.157 - glucosamine-1-phosphate N-acetyltransferase
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EC Tree
2.3.1.157 glucosamine-1-phosphate N-acetyltransferaseIUBMB Comments
The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase.
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Word Map
- 2.3.1.157
- peptidoglycan
- utp
- drug development
- tokodaii
-
left-hand
- glucosamine-6-phosphate
- glmm
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diphosphate-n-acetylglucosamine
- utase
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nucleotidylyltransferase
- udp-sugars
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
amino-sugar-1-P AcTase, amino-sugar-1-phosphate acetyltransferase, bifunctional GlmU protein, bifunctional N-acetyltransferase/uridylyltransferase, bifunctional protein GlmU, bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase, galactosamine-1-phosphate acetyltransferase, GalN-1-P AcTase, GlcN-1-P acetyltransferase, GlcN-1-P AcTase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bifunctional GlmU protein
bifunctional N-acetyltransferase/uridylyltransferase
bifunctional protein GlmU
bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase
GlcN-1-P acetyltransferase
GlcN-1-P AcTase
GlcNAc-1-P uridyltransferase
GlmU
GlmU acetyltransferase
GlmU enzyme
GlmU uridyltransferase
glucosamine 1-phosphate N-acetyltransferase/N-acetylglucosamine-1-phosphate uridyltransferase
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glucosamine-1-phosphate acetyltransferase
glucosamine-1-phosphate acetyltransferase/N-acetylglucosamine-1-phosphate uridyltransferase
MtGlmU
N-acetylglucosamine-1-phosphate uridyltransferase
N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
N-acetylglucosamine-1-phosphate-uridylyltransferase/glucosamine-1-phosphate-acetyltransferase
Rv1018c
ST0452
ST0452 protein
STK_04520
UDP-GlcNAc pyrophosphorylase
UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase
additional information
bifunctional N-acetyltransferase/uridylyltransferase
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bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase
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bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase
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GlmU
bifunctional enzyme with glucosamine 1-phosphate acetyltransferase and N-acetylglucosamine 1-phosphate uridyltransferase activities
GlmU
bifunctional enzyme with glucosamine 1-phosphate acetyltransferase and N-acetylglucosamine 1-phosphate uridyltransferase activities
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GlmU
bifunctional enzyme with glucosamine 1-phosphate acetyltransferase and N-acetylglucosamine 1-phosphate uridyltransferase activities
GlmU
bifunctional enzyme, also to possess the activity of EC 2.3.1.23, glucosamine-1-phosphate N-acetyltransferase
GlmU
bifunctional enzyme, also to possess the activity of EC 2.3.1.23, glucosamine-1-phosphate N-acetyltransferase
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GlmU
bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase
glucosamine-1-phosphate acetyltransferase
bifuncional enzyme, also N-acetylglucosamine-1-phosphate uridyltransferase activity
glucosamine-1-phosphate acetyltransferase
bifuncional enzyme, also N-acetylglucosamine-1-phosphate uridyltransferase activity
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glucosamine-1-phosphate acetyltransferase
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
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glucosamine-1-phosphate acetyltransferase/N-acetylglucosamine-1-phosphate uridyltransferase
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glucosamine-1-phosphate acetyltransferase/N-acetylglucosamine-1-phosphate uridyltransferase
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MtGlmU
bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase
MtGlmU
bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase
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N-acetylglucosamine-1-phosphate uridyltransferase
bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase
N-acetylglucosamine-1-phosphate uridyltransferase
bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase
N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
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N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
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N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
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N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
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N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
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N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
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N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
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N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
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N-acetylglucosamine-1-phosphate-uridylyltransferase/glucosamine-1-phosphate-acetyltransferase
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N-acetylglucosamine-1-phosphate-uridylyltransferase/glucosamine-1-phosphate-acetyltransferase
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N-acetylglucosamine-1-phosphate-uridylyltransferase/glucosamine-1-phosphate-acetyltransferase
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UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase
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UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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 from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase
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acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
the 2-amino group of glucosamine-1-phosphate is positioned in proximity to the acetyl-CoA to facilitate direct attack on its thioester by a ternary complex mechanism
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acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
also N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = UDP-N-acetyl-D-glucosamine + diphosphate
acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
both reactions of bifunctional GlmU follow Michaelis Menten ordered bi-bi mechanism involving an obligatory order of binding of substrates to the enzyme
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acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
substrate recognition, and catalytic mechanism for acetyltransfer involving His374, Asn397 and Ala391, overview
acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
the multifunctional enzyme from Sulfolobus tokodaii {7} 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
the catalytic mechanism is a SN2, bimolecular nucleophilic substitution reaction, catalyzed by the C-terminal domain. 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
acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
the enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase
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acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
the multifunctional enzyme from Sulfolobus tokodaii {7} 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)
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acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
also N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = UDP-N-acetyl-D-glucosamine + diphosphate
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acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:alpha-D-glucosamine-1-phosphate N-acetyltransferase
The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase.
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CAS REGISTRY NUMBER
COMMENTARY
9023-06-7
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9031-91-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
n-propionyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-propionyl-alpha-D-glucosamine 1-phosphate
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?
propionyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-propionyl-alpha-D-glucosamine 1-phosphate
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?
succinyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-succinyl-alpha-D-glucosamine 1-phosphate
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?
acetoacetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetoacetyl-alpha-D-glucosamine 1-phosphate
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?
acetoacetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetoacetyl-alpha-D-glucosamine 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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?
acetyl-CoA + alpha-D-galactosamine 1-phosphate
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
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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
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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
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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
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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
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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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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
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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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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
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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
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
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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
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
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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
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
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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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-
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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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-
-
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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
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
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)
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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
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)
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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
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
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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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-
-
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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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-
-
-
?
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
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
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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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-
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?
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
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?
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
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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
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
?
-
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
the recombinant enzyme binds to human interleukin-8, interaction analysis with human neutrophils, overview
-
-
?
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
-
-
?
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
-
-
?
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 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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-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
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
-
-
-
?
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
-
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
-
-
-
?
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
-
-
-
-
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
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
-
-
-
?
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
-
-
-
?
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
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
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
-
-
-
?
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
-
-
-
-
?
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
-
-
?
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
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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
?
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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
?
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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
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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
?
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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. 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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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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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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
Mg2+
-
absolute requirement for both activities in the sharp range from 1-10 mM with an optimal value of 3 mM
Mg2+
the concentration of Mg2+ has no effect on the enzymatic activity
Mg2+
-
has no effect on the activity of GlmU acetyltransferase up to 50 mM
Mg2+
-
required for both UDP-N-acetylglucosamine pyrophosphorylase and glucosamine-1-phosphate N-acetyltransferase activities, optimum concentration 5 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
-
(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
(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
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
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
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-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]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-[[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-([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-(1,2-oxazol-5-yl)-N-(pyridin-3-ylmethyl)furan-2-sulfonamide
44.7% inhibition at 0.1 mM
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
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
Mg2+
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
Mn2+
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
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-[(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]methanesulfonamide
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
[[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-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
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
-
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
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
-
-
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-[(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-[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-[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-([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-[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
-
-
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
MtGlmU has acetyltransferase activity in the absence of reducing agent and in the presence of a thiolreactive reagent (N-ethylmaleimide)
-
additional information
-
the enzyme is regulated by PknB via phosphorylation at Thr418 causing downregulation of acetyltransferase
-
additional information
the enzyme is regulated by PknB via phosphorylation at Thr418 causing downregulation of acetyltransferase
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Action of Dicumarol on Glucosamine-1-Phosphate Acetyltransferase of GlmU and Mycobacterium tuberculosis.
Tuberculosis
Exploring MDR-TB Inhibitory Potential of 4-Aminoquinazolines as Mycobacterium tuberculosis N-Acetylglucosamine-1-Phosphate Uridyltransferase (GlmUMTB ) Inhibitors.
Tuberculosis
Expression, essentiality, and a microtiter plate assay for mycobacterial GlmU, the bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase.
Tuberculosis
Expression, purification and preliminary crystallographic analysis of N-acetylglucosamine-1-phosphate uridylyltransferase from Mycobacterium tuberculosis.
Tuberculosis
Identification of amino acids involved in catalytic process of M. tuberculosis GlmU acetyltransferase.
Tuberculosis
Inhibition studies on Mycobacterium tuberculosis N-acetylglucosamine-1-phosphate uridyltransferase (GlmU).
Tuberculosis
Mycobacterium tuberculosis AtsG (Rv0296c), GlmU (Rv1018c) and SahH (Rv3248c) Proteins Function as the Human IL-8-Binding Effectors and Contribute to Pathogen Entry into Human Neutrophils.
Tuberculosis
PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-phosphate uridyltransferase, modulates its acetyltransferase activity.
Tuberculosis
Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group.
Tuberculosis
Structure-based design of diverse inhibitors of Mycobacterium tuberculosis N-acetylglucosamine-1-phosphate uridyltransferase: combined molecular docking, dynamic simulation, and biological activity.
Tuberculosis
The Inhibitory Effect of GlmU Acetyltransferase Inhibitor TPSA on Mycobacterium tuberculosis May Be Affected Due to Its Methylation by Methyltransferase Rv0560c.
Tuberculosis
UDP-GlcNAc pathway: Potential target for inhibitor discovery against M. tuberculosis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.056
acetyl-CoA
-
pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant K403A
0.06
acetyl-CoA
-
pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant E458A
0.07
acetyl-CoA
-
pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant S416A
0.2
acetyl-CoA
-
mutant His6GlmU, mutant His6-GlmU C296A, mutant His6-GlmU C385A
0.224
acetyl-CoA
-
pH and temperature not specified in the publication, recombinant His-tagged wild-type GlmU
0.23
acetyl-CoA
pH not specified in the publication, temperature not specified in the publication
0.242
acetyl-CoA
-
pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant S474A
0.304
acetyl-CoA
-
pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant R463A
0.343
acetyl-CoA
-
pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant N456A
0.52
acetyl-CoA
pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein
0.52
acetyl-CoA
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
1.55
acetyl-CoA
pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein
1.55
acetyl-CoA
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
0.66
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
0.84
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
1.71
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, wild-type ST0452 protein
0.008
alpha-D-glucosamine 1-phosphate
-
pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant K403A
0.016
alpha-D-glucosamine 1-phosphate
cosubstrate acetoacetyl-CoA, pH 7.5, 30°C
0.016
alpha-D-glucosamine 1-phosphate
pH 7.5, 30°C, cosubstrate: acetoacetyl-CoA
0.044
alpha-D-glucosamine 1-phosphate
-
pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant N456A
0.061
alpha-D-glucosamine 1-phosphate
-
pH and temperature not specified in the publication, recombinant His-tagged wild-type GlmU
0.066
alpha-D-glucosamine 1-phosphate
-
pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant E458A
0.069
alpha-D-glucosamine 1-phosphate
-
pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant R463A
0.073
alpha-D-glucosamine 1-phosphate
-
pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant S474A
0.107
alpha-D-glucosamine 1-phosphate
pH 7.5, 37°C, recombinant enzyme
0.107
alpha-D-glucosamine 1-phosphate
pH not specified in the publication, temperature not specified in the publication
0.13
alpha-D-glucosamine 1-phosphate
-
pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant S416A
0.241
alpha-D-glucosamine 1-phosphate
mutant enzyme C380A, at pH 8.0 and 37ðC
0.278
alpha-D-glucosamine 1-phosphate
mutant enzyme C405A, at pH 8.0 and 37ðC
0.283
alpha-D-glucosamine 1-phosphate
pH 7.6, 30°C, recombinant mutant N397A
0.29
alpha-D-glucosamine 1-phosphate
cosubstrate acetyl-CoA, pH 7.5, 30°C
0.3
alpha-D-glucosamine 1-phosphate
pH 7.6, 30°C, recombinant mutant H374A
0.3
alpha-D-glucosamine 1-phosphate
-
pH 8.2, 37°C, recombinant His6-tagged enzyme
0.304
alpha-D-glucosamine 1-phosphate
mutant enzyme V385C/C405S, at pH 8.0 and 37ðC
0.333
alpha-D-glucosamine 1-phosphate
wild type enzyme, at pH 8.0 and 37ðC
0.353
alpha-D-glucosamine 1-phosphate
pH 7.6, 30°C, recombinant wild-type
0.359
alpha-D-glucosamine 1-phosphate
mutant enzyme C405S, at pH 8.0 and 37ðC
0.37
alpha-D-glucosamine 1-phosphate
pH 7.6, 30°C, recombinant mutant S416A
0.47
alpha-D-glucosamine 1-phosphate
mutant enzyme C380A/C405S, at pH 8.0 and 37ðC
0.56
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein
0.56
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
0.59
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, wild-type enzyme
0.59
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, wild-type ST0452 protein
0.98
alpha-D-glucosamine 1-phosphate
cosubstrate propionyl-CoA, pH 7.5, 30°C
0.98
alpha-D-glucosamine 1-phosphate
pH 7.5, 30°C, cosubstrate: n-propionyl-CoA
1.69
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein
1.69
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
0.24
D-glucosamine 1-phosphate
-
Vmax: 4.489 microM/min/pmol enzyme
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
kinetic modelling of GlmU, simulation of the model, detailed overview. Estimated and measured values are very coherent
-
additional information
additional information
-
steady-state kinetics and kinetic analysis of the acetyltransferase activity of GlmU, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12.6
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
17.9
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
69.7
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, wild-type ST0452 protein
0.13
alpha-D-glucosamine 1-phosphate
cosubstrate acetoacetyl-CoA, pH 7.5, 30°C
0.13
alpha-D-glucosamine 1-phosphate
pH 7.5, 30°C, cosubstrate: acetoacetyl-CoA
0.5
alpha-D-glucosamine 1-phosphate
cosubstrate propionyl-CoA, pH 7.5, 30°C
0.5
alpha-D-glucosamine 1-phosphate
pH 7.5, 30°C, cosubstrate: n-propionyl-CoA
0.81
alpha-D-glucosamine 1-phosphate
wild type enzyme, at pH 8.0 and 37ðC
2 - 8
alpha-D-glucosamine 1-phosphate
cosubstrate acetyl-CoA, pH 7.5, 30°C
2 - 8
alpha-D-glucosamine 1-phosphate
pH 7.5, 30°C, cosubstrate: acetyl-CoA
2.407
alpha-D-glucosamine 1-phosphate
mutant enzyme C405S, at pH 8.0 and 37ðC
3.112
alpha-D-glucosamine 1-phosphate
mutant enzyme C405A, at pH 8.0 and 37ðC
15.756
alpha-D-glucosamine 1-phosphate
mutant enzyme V385C/C405S, at pH 8.0 and 37ðC
25.441
alpha-D-glucosamine 1-phosphate
mutant enzyme C380A, at pH 8.0 and 37ðC
30.783
alpha-D-glucosamine 1-phosphate
mutant enzyme C380A/C405S, at pH 8.0 and 37ðC
123.2
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, wild-type enzyme
123.2
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, wild-type ST0452 protein
490.6
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein
490.6
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
828
alpha-D-glucosamine 1-phosphate
-
pH 8.2, 37°C, recombinant His6-tagged enzyme
2311
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein
2311
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19.6
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
21.5
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
40.8
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, wild-type ST0452 protein
0.51
alpha-D-glucosamine 1-phosphate
cosubstrate propionyl-CoA, pH 7.5, 30°C
0.51
alpha-D-glucosamine 1-phosphate
pH 7.5, 30°C, cosubstrate: n-propionyl-CoA
2.432
alpha-D-glucosamine 1-phosphate
wild type enzyme, at pH 8.0 and 37ðC
6.705
alpha-D-glucosamine 1-phosphate
mutant enzyme C405S, at pH 8.0 and 37ðC
8.1
alpha-D-glucosamine 1-phosphate
cosubstrate acetoacetyl-CoA, pH 7.5, 30°C
8.1
alpha-D-glucosamine 1-phosphate
pH 7.5, 30°C, cosubstrate: acetoacetyl-CoA
11.194
alpha-D-glucosamine 1-phosphate
mutant enzyme C405A, at pH 8.0 and 37ðC
51.829
alpha-D-glucosamine 1-phosphate
mutant enzyme V385C/C405S, at pH 8.0 and 37ðC
65.496
alpha-D-glucosamine 1-phosphate
mutant enzyme C380A/C405S, at pH 8.0 and 37ðC
97
alpha-D-glucosamine 1-phosphate
cosubstrate acetyl-CoA, pH 7.5, 30°C
105.564
alpha-D-glucosamine 1-phosphate
mutant enzyme C380A, at pH 8.0 and 37ðC
211
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, wild-type enzyme
211
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, wild-type ST0452 protein
869.2
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein
869.2
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
1489
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein
1489
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0388
(5E)-1-(3,5-dimethylphenyl)-5-(furan-2-ylmethylidene)pyrimidine-2,4,6(1H,3H,5H)-trione
pH 7.5, 37°C, recombinant enzyme
0.0186
(5Z)-2-imino-5-[(2E)-3-(5-nitrofuran-2-yl)prop-2-en-1-ylidene]-1,3-thiazolidin-4-one
pH 7.5, 37°C, recombinant enzyme
0.00901
(5Z)-5-(furan-3-ylmethylidene)-1-(4-methoxyphenyl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
pH 7.5, 37°C, recombinant enzyme
0.0652
4-[[(2,6-dimethoxybenzoyl)oxy]imino]cyclohexa-2,5-dien-1-one
pH 7.5, 37°C, recombinant enzyme
0.04194
terreic acid
pH 7.6, 37°C, versus alpha-D-glucosamine 1-phosphate
0.042
terreic acid
pH 7.3, 37°C, substrate alpha-D-glucosamine 1-phosphate
additional information
additional information
-
inhibition kinetics, overview
-
additional information
additional information
inhibition kinetics, overview
-
additional information
additional information
-
inhibition kinetics, ping pong bisubstrate rate, overview
-
additional information
additional information
-
inhibition modes and kinetics, overview
-
additional information
additional information
inhibition modes and kinetics, overview
-
additional information
additional information
-
inhibition modes and kinetics, overview
-
additional information
additional information
inhibition modes and kinetics, overview
-
additional information
additional information
inhibition modes and kinetics, overview
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.01413 - 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
0.0005 - 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
0.00009 - 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
0.00009 - 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
0.0004 - 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
0.015 - 0.2
methyl 2-[([[5-(acetylamino)-2,4-dimethoxyphenyl]sulfonyl]amino)methyl]benzoate
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
0.002 - 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
0.1 - 0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]methanesulfonamide
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
0.04 - 0.2
N-[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]acetamide
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
0.0038
3-hydrazinylquinoline-2-thiol
Escherichia coli
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.1
3-hydrazinylquinoline-2-thiol
Haemophilus influenzae
pH 7.6, 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