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Enzyme Nomenclature
Information on EC 2.3.1.157 - glucosamine-1-phosphate N-acetyltransferase
for references in articles please use BRENDA:EC2.3.1.157
Word Map on EC 2.3.1.157
- 2.3.1.157
- peptidoglycan
- utp
- drug development
-
left-hand
- tokodaii
- udp-sugars
- glucosamine-6-phosphate
-
diphosphate-n-acetylglucosamine
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nucleotidylyltransferase
- medicine
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
2.3.1.157
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RECOMMENDED NAME
GeneOntology No.
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
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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; 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
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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
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
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
-
-
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
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
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
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N-acetyl-glucosamine-1-phosphate uridyltransferase, GlmU, is exclusive to prokaryotes, conserved both in Gram positive and Gram negative bacteria
evolution
-
the GlmU proteins encoded by Yersinia pestis and Yersinia pseudotuberculosis are identical in amino acid sequence
evolution
-
the GlmU proteins encoded by Yersinia pestis and Yersinia pseudotuberculosis are identical in amino acid sequence
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malfunction
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Deleting the C-terminal tail, i.e. residues 457-495, of GlmUMtb that provides these residues abolishes all acetyltransferase activity
malfunction
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GlmUMtb depletion perturbs cell wall structure and affects the bacterial survival in normoxia, overview
malfunction
-
GlmUMtb depletion perturbs cell wall structure and affects the bacterial survival in normoxia, overview
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malfunction
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GlmUMtb depletion perturbs cell wall structure and affects the bacterial survival in normoxia, overview
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metabolism
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N-acetyl-glucosamine-1-phosphate uridyltransferase, GlmU, is a bifunctional enzyme involved in bacterial cell wall synthesis
metabolism
-
the enzymeis involved in the UDP-N-acetylglucosamine synthesis pathway, overview
metabolism
-
the enzymeis involved in the UDP-N-acetylglucosamine synthesis pathway, overview
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physiological function
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essentiality of GlmU to mycobacterial survival
physiological function
-
the C-terminal domain of bifunctional GlmU catalyzes the transfer of an acetyl group from acetyl coenzyme A to glucosamine-1-phosphate to produce N-acetylglucosamine-1-phosphate. In the second step, the N-terminal domain of GlmU catalyzes the transfer of uridyl monophosphate from UTP to acetylglucosamine-1-phosphate to produce UDP-GlcNAc and diphosphate
physiological function
-
the C-terminal domain of bifunctional GlmU catalyzes the transfer of an acetyl group from acetyl coenzyme A to glucosamine-1-phosphate to produce N-acetylglucosamine-1-phosphate. In the second step, the N-terminal domain of GlmU catalyzes the transfer of uridyl monophosphate from UTP to acetylglucosamine-1-phosphate to produce UDP-GlcNAc and diphosphate
physiological function
-
the C-terminal domain of bifunctional GlmU catalyzes the transfer of an acetyl group from acetyl coenzyme A to glucosamine-1-phosphate to produce N-acetylglucosamine-1-phosphate. In the second step, the N-terminal domain of GlmU catalyzes the transfer of uridyl monophosphate from UTP to acetylglucosamine-1-phosphate to produce UDP-GlcNAc and diphosphate
physiological function
-
the C-terminal domain of bifunctional GlmU catalyzes the transfer of an acetyl group from acetyl coenzyme A to glucosamine-1-phosphate to produce N-acetylglucosamine-1-phosphate. In the second step, the N-terminal domain of GlmU catalyzes the transfer of uridyl monophosphate from UTP to acetylglucosamine-1-phosphate to produce UDP-GlcNAc and diphosphate
physiological function
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the bifunctional enzyme N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, catalyzes two-step formation of UDP-GlcNAc, an important precursor in bacterial peptidoglycan and lipopolysaccharide biosynthesis, which are important constituents of the cell wall of both Gram-positive and Gram-negative bacteria. The first activity of GlmU, the C-terminal domain (acetyltransferase), catalyzes the formation of N-acetylglucosamine-1-phosphate from glucosamine-1-phosphate using acetyl-CoA as the acetyl donor. The second activity of GlmU, the N-terminal and rate-limiting domain (uridyltransferase), catalyzes the formation of UDP-GlcNAc from GlcNAc-1-phosphate and uridine triphosphate, UTP
physiological function
-
GlmU is a bifunctional enzyme with acetyltransferase activity in C-terminus, residues 251-495, and uridyltransferase activity in N-terminus, and it is involved in the biosynthesis of glycosyl donor UDP-N-acetylglucosamine
physiological function
-
GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
physiological function
-
GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
physiological function
-
GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
physiological function
-
GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
physiological function
-
GlmU is involved in the biosynthesis of UDP-N-acetylglucosamine-1-phosphate. It is a bifunctional protein with two independent active sites catalyzing acetyl transfer and uridyl transfer reactions on glucosamine-1-phosphate. It synthesizes two key intermediates of cell wall biosynthesis pathways, viz. N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc. The acetyltransferase activity is catalyzed by the C-terminal domain. It is essential for the growth of the organism; N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme involved in bacterial cell wall synthesis and is exclusive to prokaryotes. The enzyme is regulated by PknB via phosphorylation at Thr418 causing downregulation of acetyltransferase
physiological function
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the C- and N-terminal domains of bifunctional enzyme mycobacterial glucosamine 1-phosphate N-acetyltransferase/N-acetylglucosamine-1-phosphate uridyltransferase catalyze acetyltransferase and uridyltransferase (cf. EC 2.7.7.23) activities, respectively, and the final product is involved in peptidoglycan synthesis
physiological function
-
because the ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
physiological function
-
the archaeal enzyme's high GalN-1-P AcTase activity, which is not detected on the bacterial and eukaryotic similar enzymes, supports the production of the UDP-GalNAc in archaeal cells
physiological function
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the bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase enzyme GlmU is an essential gene in Yersinia
physiological function
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the enzyme is one of the pathogen proteins that bind to human interleukin-8, IL-8. The binding interaction of mycobacterial proteins AtsG, GlmU and SahH with human IL-8 may indicate that these proteins participate in the modulation of the early events of infection with tubercle bacilli and could affect pathogen attachment to target cells. Interleukin-8 belongs to the family of CXC chemokines and functions as a chemoattractant and activator of different subsets of leukocytes
physiological function
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absence of GlmU leads to extensive perturbation of bacterial morphology and substantial reduction in cell wall thickness under normoxic as well as hypoxic conditions. The acetyl- and uridyl-transferase activities of GlmU are independently essential for bacterial survival in vitro, and GlmU is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. Depletion of GlmU from infected murine lungs, four weeks post infection, leads to significant reduction in the bacillary load; the acetyl- and uridyltransferase activities of GlmUMtb are independently essential for bacterial survival in vitro, and GlmUMtb is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. The administration of Oxa33, a novel oxazolidine derivative that specifically inhibits GlmUMtb, to infected mice results in significant decrease in the bacillary load. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively
physiological function
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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. Final product of GlmU catalyzed reaction, uridine-diphospho-N-acetylglucosamine (UDP-GlcNAc), acts as sugar donor providing GlcNAc residues in the synthesis of peptidoglycan and a disaccharide linker (D-N-GlcNAc-1-rhamnose), the key structural components of Mycobacterium tuberculosis cell wall
physiological function
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GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
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physiological function
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GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
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physiological function
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absence of GlmU leads to extensive perturbation of bacterial morphology and substantial reduction in cell wall thickness under normoxic as well as hypoxic conditions. The acetyl- and uridyl-transferase activities of GlmU are independently essential for bacterial survival in vitro, and GlmU is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. Depletion of GlmU from infected murine lungs, four weeks post infection, leads to significant reduction in the bacillary load; the acetyl- and uridyltransferase activities of GlmUMtb are independently essential for bacterial survival in vitro, and GlmUMtb is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. The administration of Oxa33, a novel oxazolidine derivative that specifically inhibits GlmUMtb, to infected mice results in significant decrease in the bacillary load. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively; the enzyme is one of the pathogen proteins that bind to human interleukin-8, IL-8. The binding interaction of mycobacterial proteins AtsG, GlmU and SahH with human IL-8 may indicate that these proteins participate in the modulation of the early events of infection with tubercle bacilli and could affect pathogen attachment to target cells. Interleukin-8 belongs to the family of CXC chemokines and functions as a chemoattractant and activator of different subsets of leukocytes
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physiological function
-
absence of GlmU leads to extensive perturbation of bacterial morphology and substantial reduction in cell wall thickness under normoxic as well as hypoxic conditions. The acetyl- and uridyl-transferase activities of GlmU are independently essential for bacterial survival in vitro, and GlmU is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. Depletion of GlmU from infected murine lungs, four weeks post infection, leads to significant reduction in the bacillary load; N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively. Final product of GlmU catalyzed reaction, uridine-diphospho-N-acetylglucosamine (UDP-GlcNAc), acts as sugar donor providing GlcNAc residues in the synthesis of peptidoglycan and a disaccharide linker (D-N-GlcNAc-1-rhamnose), the key structural components of Mycobacterium tuberculosis cell wall; the acetyl- and uridyltransferase activities of GlmUMtb are independently essential for bacterial survival in vitro, and GlmUMtb is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. The administration of Oxa33, a novel oxazolidine derivative that specifically inhibits GlmUMtb, to infected mice results in significant decrease in the bacillary load. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively; the enzyme is one of the pathogen proteins that bind to human interleukin-8, IL-8. The binding interaction of mycobacterial proteins AtsG, GlmU and SahH with human IL-8 may indicate that these proteins participate in the modulation of the early events of infection with tubercle bacilli and could affect pathogen attachment to target cells. Interleukin-8 belongs to the family of CXC chemokines and functions as a chemoattractant and activator of different subsets of leukocytes
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physiological function
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GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
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physiological function
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GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
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physiological function
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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; the archaeal enzyme's high GalN-1-P AcTase activity, which is not detected on the bacterial and eukaryotic similar enzymes, supports the production of the UDP-GalNAc in archaeal cells
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physiological function
Sulfolobus tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
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the archaeal enzyme's high GalN-1-P AcTase activity, which is not detected on the bacterial and eukaryotic similar enzymes, supports the production of the UDP-GalNAc in archaeal cells
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physiological function
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the bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase enzyme GlmU is an essential gene in Yersinia
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additional information
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analysis of structures of GlmUMtb bound to substrates of the acetyl transfer reaction; the catalytic mechanism operative in GlmUMtb performs a SN2 reaction, His374 and Asn397 act as catalytic residues by enhancing the nucleophilicity of the attacking amino group of glucosamine 1-phosphate. Ser416 and Trp460, on a short helix, provide important interactions for substrate binding. The enzyme shows an uncommon mode of binding with acetyl-CoA. GlmU from Mycobacterium tuberculosis possesses a unique 30-residue extension at the C-terminus. The adenine base of acetyl-CoA bound to GlmUMtb is buried at the interface of two monomers of the trimer
additional information
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the C-terminal tail region of the ST0452 protein might be important for recognition of the multiple substrates for amino-sugar-1-P AcTase activity. The ST0452 protein contains only two Cys residues, it is unlikely that Cys-Cys bonds contribute to its thermostability. Residue Asn331 in the ST0452 protein is essential for the GalN-1-P AcTase activity, but it is much less important and not essential for the GlcN-1-P AcTase activity. The C-terminal residues of the ST0452 protein enhance the turnover rate of its GalN-1-P AcTase catalytic activity and slightly suppress substrate binding. Residue H308 is essential for both amino-sugar-1-P AcTase activities of the ST0452 protein
additional information
-
the C-terminal tail region of the ST0452 protein might be important for recognition of the multiple substrates for amino-sugar-1-P AcTase activity. The ST0452 protein contains only two Cys residues, it is unlikely that Cys-Cys bonds contribute to its thermostability. Residue Asn331 in the ST0452 protein is essential for the GalN-1-P AcTase activity, but it is much less important and not essential for the GlcN-1-P AcTase activity. The C-terminal residues of the ST0452 protein enhance the turnover rate of its GalN-1-P AcTase catalytic activity and slightly suppress substrate binding. Residue H308 is essential for both amino-sugar-1-P AcTase activities of the ST0452 protein
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additional information
Sulfolobus tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
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the C-terminal tail region of the ST0452 protein might be important for recognition of the multiple substrates for amino-sugar-1-P AcTase activity. The ST0452 protein contains only two Cys residues, it is unlikely that Cys-Cys bonds contribute to its thermostability. Residue Asn331 in the ST0452 protein is essential for the GalN-1-P AcTase activity, but it is much less important and not essential for the GlcN-1-P AcTase activity. The C-terminal residues of the ST0452 protein enhance the turnover rate of its GalN-1-P AcTase catalytic activity and slightly suppress substrate binding. Residue H308 is essential for both amino-sugar-1-P AcTase activities of the ST0452 protein
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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
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
Sulfolobus 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
-
-
-
-
?
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
-
uncommon mode of acetyl-CoA binding in GlmUMtb in the U conformation, which is distinct from the L conformation seen in the available non-mycobacterial GlmU structures. Higly conserved Trp460 is critical for acetyl-CoA binding
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
because the ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
no activity with alpha-D-glucosamine 6-phosphate. The multifunctional enzyme is also active with acetyl-CoA + alpha-D-galactosamine 1-phosphate (galactosamine-1-phosphate N-acetyltransferase), UTP + N-acetylglucosamine 1-phosphate (EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase) and UTP + N-acetyl-alpha-D-galactosamine 1-phosphate (EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase)
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
because the ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
no activity with alpha-D-glucosamine 6-phosphate. The multifunctional enzyme is also active with acetyl-CoA + alpha-D-galactosamine 1-phosphate (galactosamine-1-phosphate N-acetyltransferase), UTP + N-acetylglucosamine 1-phosphate (EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase) and UTP + N-acetyl-alpha-D-galactosamine 1-phosphate (EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase)
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
Sulfolobus 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
-
-
-
-
?
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
-
-
-
-
-
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
the bifunctional enzyme also possesses the activity of EC 2.7.7.23. The C-terminal domain is responsible for the CoA-dependent acetylation of Glc-1-phosphate to GlcNAc-1-phosphate. The N-terminal domain catalyzes uridyl transfer from UTP to GlcNAc-1-phosphate to form the final products UDP-GlcNAc and pyrophosphate
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
-
presence of acetyl-coenzyme A has an inhibitory effect on uridyltransferase activity of the bifunctional enzyme
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
-
presence of acetyl-coenzyme A has an inhibitory effect on uridyltransferase activity of the bifunctional enzyme
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
-
-
-
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine, which is an essential precursor in bacterial cell wall biosynthesis
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
-
the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine, which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathway
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
-
a mechanism is proposed in which the activation energy of the double negatively charged phosphorane transition state is lowered by charge compensation of Mg2+ and the side-chain of Lys22
-
-
?
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetylglucosamine + ?
-
-
-
-
-
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetylglucosamine + ?
-
-
-
-
?
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-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
UDP-N-acetylglucosamine + H2O
N-acetyl-D-glucosamine 1-phosphate + UMP
-
-
-
-
r
UDP-N-acetylglucosamine + H2O
N-acetyl-D-glucosamine 1-phosphate + UMP
-
-
-
-
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
?
-
-
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-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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
Sulfolobus 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 SUBSTRATES
NATURAL PRODUCTS
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
Sulfolobus tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
Q975F9
-
-
-
?
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
P0ACC7
-
-
-
?
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
P0ACC7
-
-
-
?
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
P43889
-
-
-
?
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
P43889
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
r
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
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
Q975F9
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
Q975F9
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
Sulfolobus tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
Q975F9
-
-
-
?
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
-
-
-
-
-
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
P0ACC7
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
-
-
-
-
-
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
Q97R46
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
?
-
P0ACC7
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
?
-
P0ACC7
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
?
-
P43889
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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P43889
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-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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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+
Mg2+
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absolute requirement for both activities in the sharp range from 1-10 mM with an optimal value of 3 mM
Mg2+
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has no effect on the activity of GlmU acetyltransferase up to 50 mM
Mg2+
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required for both UDP-N-acetylglucosamine pyrophosphorylase and glucosamine-1-phosphate N-acetyltransferase activities, optimum concentration 5 mM
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INHIBITORS
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
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(4Z)-4-(4-benzyloxybenzylidene)-2-(naphthalen-2-yl)-1,3-oxazol-5(4H)-one
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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
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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
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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
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unspecific inhibitor, 84.26% inhibition at 0.1 mM
1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenylamino]-2-(4-pyridyl)-1-ethanone
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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
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40.0% inhibition at 0.1 mM
4-(4-(benzyloxy)benzylidene)-2-(naphthalen-1-yl)oxazol-5(4H)-one
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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
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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
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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
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44.7% inhibition at 0.1 mM
alpha-D-glucosamine 1-phosphate
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substrate inhibition, competitive versus N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
Ca2+
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2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
Co2+
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2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
ethyl (2-[(Z)-[2-(ethylsulfanyl)-5-oxo-1,3-thiazol-4(5H)-ylidene]methyl]phenoxy)acetate
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45.3% inhibition at 0.1 mM
Mg2+
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2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
Mn2+
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2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
N-(2,5-dimethoxyphenyl)-N-(phenylsulfonyl)glycine
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42.01% inhibition at 0.1 mM
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N-(3-chlorophenyl)-2-methoxy-5-(2-methyl-1,3-oxazol-5-yl)benzenesulfonamide
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406% inhibition at 0.1 mM
N-(5-chloro-2-methoxyphenyl)-N-(phenylsulfonyl)glycine
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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
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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
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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
terreic acid
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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
Zn2+
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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
[[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
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(1R,2R)-2-[[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
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(1R,2R)-2-[[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
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(1R,2R)-2-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
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(1R,2R)-2-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
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(1R,2R)-2-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
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(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
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(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
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(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
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(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-4-hydroxy-2-methoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
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(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-4-hydroxy-2-methoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
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(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-4-hydroxy-2-methoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
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(2E)-4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobut-2-enoic acid
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(2E)-4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobut-2-enoic acid
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(2E)-4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobut-2-enoic acid
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(2E)-4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobut-2-enoic acid
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(E)-N-(2,5-dimethylphenyl)-1-(5-nitrofuran-2-yl)methanimine
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specific inhibitor, 93.82% inhibition at 0.1 mM
(E)-N-(2-fluoro-5-nitrophenyl)-1-(5-nitrofuran-2-yl)methanimine
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specific inhibitor, 97.47% inhibition at 0.1 mM
(E)-N-(2-fluoro-5-nitrophenyl)-1-(5-nitrofuran-2-yl)methanimine
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1-(2-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]phenyl)piperidine-4-carboxylic acid
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1-(2-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]phenyl)piperidine-4-carboxylic acid
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1-(2-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]phenyl)piperidine-4-carboxylic acid
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1-(2-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]phenyl)piperidine-4-carboxylic acid
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2'-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]biphenyl-4-carboxylic acid
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2'-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]biphenyl-4-carboxylic acid
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2'-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]biphenyl-4-carboxylic acid
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2'-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]biphenyl-4-carboxylic acid
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2-(2-cyanopyridin-4-yl)-N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]acetamide
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2-(2-cyanopyridin-4-yl)-N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]acetamide
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2-(2-cyanopyridin-4-yl)-N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]acetamide
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2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl acetate
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2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl acetate
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2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl acetate
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2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl acetate
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3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzenesulfonamide
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specific inhibitor, 82.87% inhibition at 0.1 mM
3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzenesulfonamide
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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
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3-hydrazinylquinoline-2-thiol
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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
4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
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4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
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4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
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4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
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4-([2,4-dimethoxy-5-[naphthalen-2-yl(phenyl)sulfamoyl]phenyl]amino)-4-oxobutanoic acid
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4-([2,4-dimethoxy-5-[naphthalen-2-yl(phenyl)sulfamoyl]phenyl]amino)-4-oxobutanoic acid
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4-([2,4-dimethoxy-5-[naphthalen-2-yl(phenyl)sulfamoyl]phenyl]amino)-4-oxobutanoic acid
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4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
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4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
-
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4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
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4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
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4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
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4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
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4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
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4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
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4-([5-[bis(4-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
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4-([5-[bis(4-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
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4-([5-[bis(4-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
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4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
-
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4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
-
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4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
-
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4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
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4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
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4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
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4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
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4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
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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
-
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
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
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-[(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
-
-
[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
-
-
[[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, 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 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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 7.5, 37°C, recombinant enzyme; 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
0.355
acetyl-CoA
-
pH 7.6, 30°C, recombinant mutant N397A; pH 7.6, 30°C, recombinant mutant S416A; pH 7.6, 30°C, recombinant wild-type
0.52
acetyl-CoA
-
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein
0.63
acetyl-CoA
-
pH 7.5, 80°C, wild-type enzyme; pH 7.5, 80°C, wild-type ST0452 protein
1.55
acetyl-CoA
-
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the 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
0.044
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; 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
0.283
alpha-D-glucosamine 1-phosphate
-
pH 7.6, 30°C, recombinant mutant N397A
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
0.353
alpha-D-glucosamine 1-phosphate
-
pH 7.6, 30°C, recombinant wild-type
0.37
alpha-D-glucosamine 1-phosphate
-
pH 7.6, 30°C, recombinant mutant S416A
0.56
alpha-D-glucosamine 1-phosphate
-
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein
0.59
alpha-D-glucosamine 1-phosphate
-
pH 7.5, 80°C, wild-type enzyme; pH 7.5, 80°C, wild-type ST0452 protein
1.69
alpha-D-glucosamine 1-phosphate
-
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein
0.24
D-glucosamine 1-phosphate
-
Vmax: 4.489 microM/min/pmol enzyme
additional information
additional information
-
steady-state kinetics and kinetic analysis of the acetyltransferase activity of GlmU, overview
-
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
-
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
123.2
alpha-D-glucosamine 1-phosphate
-
pH 7.5, 80°C, wild-type enzyme; pH 7.5, 80°C, wild-type ST0452 protein
490.6
alpha-D-glucosamine 1-phosphate
-
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the 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, deletion mutant D011 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the 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
211
alpha-D-glucosamine 1-phosphate
-
pH 7.5, 80°C, wild-type enzyme; pH 7.5, 80°C, wild-type ST0452 protein
869.2
alpha-D-glucosamine 1-phosphate
-
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein
1489
alpha-D-glucosamine 1-phosphate
-
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein; pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the 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
0.042
terreic acid
-
pH 7.3, 37°C, substrate alpha-D-glucosamine 1-phosphate
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 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 - 0.0485
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
0.002 - 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
0.0001 - 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
0.01413
(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;
P43889
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;
P43889
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
Escherichia coli;
-
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
Haemophilus influenzae;
-
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]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;
P43889
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;
P43889
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.00009
4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
Escherichia coli;
-
pH 7.35, 22°C
0.0006
4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
Haemophilus influenzae;
-
pH 7.35, 22°C
0.02
4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
Streptococcus pneumoniae;
-
pH 7.35, 22°C
0.2
4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.00004
4-([2,4-dimethoxy-5-[naphthalen-2-yl(phenyl)sulfamoyl]phenyl]amino)-4-oxobutanoic acid
Escherichia coli;
-
pH and temperature not specified in the publication
0.00083
4-([2,4-dimethoxy-5-[naphthalen-2-yl(phenyl)sulfamoyl]phenyl]amino)-4-oxobutanoic acid
Haemophilus influenzae;
-
pH and temperature not specified in the publication
0.0084
4-([2,4-dimethoxy-5-[naphthalen-2-yl(phenyl)sulfamoyl]phenyl]amino)-4-oxobutanoic acid
Streptococcus pneumoniae;
-
pH and temperature not specified in the publication
0.000058
4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
Escherichia coli;
-
pH 7.2, temperature not specified in the publication
0.00028
4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
Haemophilus influenzae;
-
pH 7.2, temperature not specified in the publication
0.0047
4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
Streptococcus pneumoniae;
-
pH 7.2, temperature not specified in the publication
0.2
4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
Staphylococcus aureus;
-
above, pH 7.2, temperature not specified in the publication
0.000018
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Escherichia coli;
-
pH 7.2, temperature not specified in the publication
0.00002
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Escherichia coli;
-
pH and temperature not specified in the publication
0.0004
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Haemophilus influenzae;
-
pH and temperature not specified in the publication
0.0004
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Haemophilus influenzae;
-
pH 7.2, temperature not specified in the publication
0.04
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Streptococcus pneumoniae;
-
pH 7.2, temperature not specified in the publication
0.0402
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Streptococcus pneumoniae;
-
pH and temperature not specified in the publication
0.2
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Staphylococcus aureus;
-
above, pH 7.2, temperature not specified in the publication
0.00004
4-([5-[bis(4-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Escherichia coli;
-
pH and temperature not specified in the publication
0.00032
4-([5-[bis(4-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Haemophilus influenzae;
-
pH and temperature not specified in the publication
0.048
4-([5-[bis(4-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Streptococcus pneumoniae;
-
pH and temperature not specified in the publication
0.003
4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
Escherichia coli;
-
pH 7.35, 22°C
0.005
4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
Haemophilus influenzae;
-
pH 7.35, 22°C
0.012
4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
Streptococcus pneumoniae;
-
pH 7.35, 22°C
0.2
4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.00025
4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
Escherichia coli;
-
pH 7.35, 22°C
0.0005
4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
Haemophilus influenzae;
-
pH 7.35, 22°C
0.0005
4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
Streptococcus pneumoniae;
-
pH 7.35, 22°C
0.2
4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
4-[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]benzoic acid
Escherichia coli;
-
above, pH 7.35, 22°C
0.2
4-[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]benzoic acid
Haemophilus influenzae;
-
above, pH 7.35, 22°C
0.2
4-[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]benzoic acid
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
4-[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]benzoic acid
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.0322
4-[[(2,6-dimethoxybenzoyl)oxy]imino]cyclohexa-2,5-dien-1-one
Mycobacterium tuberculosis;
-
versus alpha-D-glucosamine 1-phosphate, pH 7.5, 37°C, recombinant enzyme
0.0533
4-[[(2,6-dimethoxybenzoyl)oxy]imino]cyclohexa-2,5-dien-1-one
Mycobacterium tuberculosis;
-
versus acetyl-CoA, pH 7.5, 37°C, recombinant enzyme
0.065
4-[[(2,6-dimethoxybenzoyl)oxy]imino]cyclohexa-2,5-dien-1-one
Mycobacterium tuberculosis;
-
pH not specified in the publication, temperature not specified in the publication
0.00009
4-[[2,4-dimethoxy-5-(10H-phenothiazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Escherichia coli;
-
pH and temperature not specified in the publication
0.00037
4-[[2,4-dimethoxy-5-(10H-phenothiazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Haemophilus influenzae;
-
pH and temperature not specified in the publication
0.0369
4-[[2,4-dimethoxy-5-(10H-phenothiazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Streptococcus pneumoniae;
-
pH and temperature not specified in the publication
0.000007
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Escherichia coli;
-
pH 7.2, temperature not specified in the publication
0.00001
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Escherichia coli;
-
pH and temperature not specified in the publication
0.00001
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Escherichia coli;
-
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.00002
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Haemophilus influenzae;
-
pH and temperature not specified in the publication
0.000023
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Haemophilus influenzae;
-
pH 7.2, temperature not specified in the publication
0.0146
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Streptococcus pneumoniae;
-
pH and temperature not specified in the publication
0.015
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Streptococcus pneumoniae;
-
pH 7.2, temperature not specified in the publication
0.0215
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Streptococcus pneumoniae;
-
pH and temperature not specified in the publication
0.2
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Staphylococcus aureus;
-
above, pH 7.2, temperature not specified in the publication
0.00005
4-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Escherichia coli;
-
pH and temperature not specified in the publication
0.00028
4-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Haemophilus influenzae;
-
pH and temperature not specified in the publication
0.0466
4-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Streptococcus pneumoniae;
-
pH and temperature not specified in the publication
0.00003
4-[[5-(dibenzo[b,f][1,4]oxazepin-10(11H)-ylsulfonyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Escherichia coli;
-
pH and temperature not specified in the publication
0.00008
4-[[5-(dibenzo[b,f][1,4]oxazepin-10(11H)-ylsulfonyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Haemophilus influenzae;
-
pH and temperature not specified in the publication
0.055
4-[[5-(dibenzo[b,f][1,4]oxazepin-10(11H)-ylsulfonyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Streptococcus pneumoniae;
-
pH and temperature not specified in the publication
0.00004
4-[[5-(diphenylsulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Escherichia coli;
-
pH and temperature not specified in the publication
0.00091
4-[[5-(diphenylsulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Haemophilus influenzae;
-
pH and temperature not specified in the publication
0.0255
4-[[5-(diphenylsulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Streptococcus pneumoniae;
-
pH and temperature not specified in the publication
0.0004
4-[[5-([2-[4-(carboxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Escherichia coli;
-
pH 7.35, 22°C
0.002
4-[[5-([2-[4-(carboxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Streptococcus pneumoniae;
-
pH 7.35, 22°C
0.003
4-[[5-([2-[4-(carboxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Haemophilus influenzae;
-
pH 7.35, 22°C
0.01
4-[[5-([2-[4-(carboxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Staphylococcus aureus;
-
pH 7.35, 22°C
0.003
4-[[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Escherichia coli;
-
pH 7.35, 22°C
0.005
4-[[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Streptococcus pneumoniae;
-
pH 7.35, 22°C
0.006
4-[[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Haemophilus influenzae;
-
pH 7.35, 22°C
0.2
4-[[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.0014
5,7-dichloro-2-hydrazinylquinolin-8-ol
Escherichia coli;
-
pH 7.6, 30°C, recombinant His6-tagged enzyme; pH not specified in the publication, temperature not specified in the publication
0.0799
5,7-dichloro-2-hydrazinylquinolin-8-ol
Haemophilus influenzae;
P43889
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.015
methyl 2-[([[5-(acetylamino)-2,4-dimethoxyphenyl]sulfonyl]amino)methyl]benzoate
Escherichia coli;
-
pH 7.35, 22°C
0.055
methyl 2-[([[5-(acetylamino)-2,4-dimethoxyphenyl]sulfonyl]amino)methyl]benzoate
Haemophilus influenzae;
-
pH 7.35, 22°C
0.2
methyl 2-[([[5-(acetylamino)-2,4-dimethoxyphenyl]sulfonyl]amino)methyl]benzoate
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
methyl 2-[([[5-(acetylamino)-2,4-dimethoxyphenyl]sulfonyl]amino)methyl]benzoate
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.11
N-(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)acetamide
Streptococcus pneumoniae;
-
pH 7.35, 22°C
0.12
N-(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)acetamide
Haemophilus influenzae;
-
pH 7.35, 22°C
0.2
N-(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)acetamide
Escherichia coli;
-
above, pH 7.35, 22°C
0.2
N-(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.0005
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamothioyl)glycine
Escherichia coli;
-
pH 7.35, 22°C
0.001
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamothioyl)glycine
Haemophilus influenzae;
-
pH 7.35, 22°C
0.03
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamothioyl)glycine
Streptococcus pneumoniae;
-
pH 7.35, 22°C
0.2
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamothioyl)glycine
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.0005
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamoyl)glycine
Escherichia coli;
-
pH 7.35, 22°C
0.005
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamoyl)glycine
Haemophilus influenzae;
-
pH 7.35, 22°C
0.02
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamoyl)glycine
Streptococcus pneumoniae;
-
pH 7.35, 22°C
0.2
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamoyl)glycine
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.00052
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-2-(2-fluoropyridin-4-yl)acetamide
Haemophilus influenzae;
-
pH and temperature not specified in the publication
0.0008
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-2-(2-fluoropyridin-4-yl)acetamide
Escherichia coli;
-
pH and temperature not specified in the publication
0.009
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-2-(2-fluoropyridin-4-yl)acetamide
Streptococcus pneumoniae;
-
pH and temperature not specified in the publication
0.00043
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-3-(2H-tetrazol-5-yl)propanamide
Escherichia coli;
-
pH and temperature not specified in the publication
0.0006
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-3-(2H-tetrazol-5-yl)propanamide
Haemophilus influenzae;
-
pH and temperature not specified in the publication
0.0247
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-3-(2H-tetrazol-5-yl)propanamide
Streptococcus pneumoniae;
-
pH and temperature not specified in the publication
0.07
N-[2,4-dimethoxy-5-(phenylsulfamoyl)phenyl]acetamide
Haemophilus influenzae;
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-(phenylsulfamoyl)phenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-(phenylsulfamoyl)phenyl]acetamide
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.08
N-[2,4-dimethoxy-5-(piperidin-1-ylsulfonyl)phenyl]acetamide
Escherichia coli;
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-(piperidin-1-ylsulfonyl)phenyl]acetamide
Haemophilus influenzae;
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-(piperidin-1-ylsulfonyl)phenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-(piperidin-1-ylsulfonyl)phenyl]acetamide
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.01
N-[2,4-dimethoxy-5-[(2-methoxybenzyl)sulfamoyl]phenyl]acetamide
Escherichia coli;
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methoxybenzyl)sulfamoyl]phenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methoxybenzyl)sulfamoyl]phenyl]acetamide
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.54
N-[2,4-dimethoxy-5-[(2-methoxybenzyl)sulfamoyl]phenyl]acetamide
Haemophilus influenzae;
-
pH 7.35, 22°C
0.002
N-[2,4-dimethoxy-5-[(2-methyl-2,3-dihydro-1H-indol-1-yl)sulfonyl]phenyl]acetamide
Escherichia coli;
-
pH 7.35, 22°C
0.008
N-[2,4-dimethoxy-5-[(2-methyl-2,3-dihydro-1H-indol-1-yl)sulfonyl]phenyl]acetamide
Haemophilus influenzae;
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-2,3-dihydro-1H-indol-1-yl)sulfonyl]phenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-2,3-dihydro-1H-indol-1-yl)sulfonyl]phenyl]acetamide
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.001
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]-2-(pyridin-4-ylsulfanyl)acetamide
Escherichia coli;
-
pH 7.35, 22°C
0.006
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]-2-(pyridin-4-ylsulfanyl)acetamide
Haemophilus influenzae;
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]-2-(pyridin-4-ylsulfanyl)acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]-2-(pyridin-4-ylsulfanyl)acetamide
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.0015
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
Escherichia coli;
-
pH 7.35, 22°C
0.0021
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
Escherichia coli;
-
pH 7.2, temperature not specified in the publication
0.003
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
Haemophilus influenzae;
-
pH 7.35, 22°C
0.0078
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
Haemophilus influenzae;
-
pH 7.2, temperature not specified in the publication
0.055
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
Streptococcus pneumoniae;
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.2, temperature not specified in the publication
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
Streptococcus pneumoniae;
-
above, pH 7.2, temperature not specified in the publication
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]benzamide
Escherichia coli;
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]benzamide
Haemophilus influenzae;
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]benzamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]benzamide
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.1
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]methanesulfonamide
Escherichia coli;
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]methanesulfonamide
Haemophilus influenzae;
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]methanesulfonamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]methanesulfonamide
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methylpyrrolidin-1-yl)sulfonyl]phenyl]acetamide
Escherichia coli;
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methylpyrrolidin-1-yl)sulfonyl]phenyl]acetamide
Haemophilus influenzae;
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methylpyrrolidin-1-yl)sulfonyl]phenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methylpyrrolidin-1-yl)sulfonyl]phenyl]acetamide
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.017
N-[2,4-dimethoxy-5-[(3-methylphenyl)sulfamoyl]phenyl]acetamide
Escherichia coli;
-
pH 7.35, 22°C
0.04
N-[2,4-dimethoxy-5-[(3-methylphenyl)sulfamoyl]phenyl]acetamide
Haemophilus influenzae;
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(3-methylphenyl)sulfamoyl]phenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(3-methylphenyl)sulfamoyl]phenyl]acetamide
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.021
N-[2,4-dimethoxy-5-[(4-methylphenyl)sulfamoyl]phenyl]acetamide
Escherichia coli;
-
pH 7.35, 22°C
0.047
N-[2,4-dimethoxy-5-[(4-methylphenyl)sulfamoyl]phenyl]acetamide
Haemophilus influenzae;
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(4-methylphenyl)sulfamoyl]phenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(4-methylphenyl)sulfamoyl]phenyl]acetamide
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.003
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
Escherichia coli;
-
pH 7.35, 22°C
0.0033
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
Escherichia coli;
-
pH 7.2, temperature not specified in the publication
0.006
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
Haemophilus influenzae;
-
pH 7.35, 22°C
0.0064
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
Haemophilus influenzae;
-
pH 7.2, temperature not specified in the publication
0.2
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.2, temperature not specified in the publication
0.2
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
Streptococcus pneumoniae;
-
above, pH 7.2, temperature not specified in the publication
0.002
N-[2,4-dimethoxy-5-[phenyl(propan-2-yl)sulfamoyl]phenyl]acetamide
Escherichia coli;
-
pH 7.35, 22°C
0.016
N-[2,4-dimethoxy-5-[phenyl(propan-2-yl)sulfamoyl]phenyl]acetamide
Haemophilus influenzae;
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[phenyl(propan-2-yl)sulfamoyl]phenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[phenyl(propan-2-yl)sulfamoyl]phenyl]acetamide
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.00003
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(2-fluoropyridin-4-yl)acetamide
Haemophilus influenzae;
-
pH and temperature not specified in the publication
0.00009
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(2-fluoropyridin-4-yl)acetamide
Escherichia coli;
-
pH and temperature not specified in the publication
0.0099
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(2-fluoropyridin-4-yl)acetamide
Streptococcus pneumoniae;
-
pH and temperature not specified in the publication
0.00003
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(pyridin-4-yl)acetamide
Haemophilus influenzae;
-
pH and temperature not specified in the publication
0.00006
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(pyridin-4-yl)acetamide
Escherichia coli;
-
pH and temperature not specified in the publication
0.032
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(pyridin-4-yl)acetamide
Streptococcus pneumoniae;
-
pH and temperature not specified in the publication
0.2
N-[5-(dimethylsulfamoyl)-2,4-dimethoxyphenyl]acetamide
Escherichia coli;
-
above, pH 7.35, 22°C
0.2
N-[5-(dimethylsulfamoyl)-2,4-dimethoxyphenyl]acetamide
Haemophilus influenzae;
-
above, pH 7.35, 22°C
0.2
N-[5-(dimethylsulfamoyl)-2,4-dimethoxyphenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[5-(dimethylsulfamoyl)-2,4-dimethoxyphenyl]acetamide
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.04
N-[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]acetamide
Escherichia coli;
-
pH 7.35, 22°C
0.07
N-[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]acetamide
Streptococcus pneumoniae;
-
pH 7.35, 22°C
0.08
N-[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]acetamide
Haemophilus influenzae;
-
pH 7.35, 22°C
0.2
N-[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[5-[(1,3-benzodioxol-5-ylmethyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli;
-
above, pH 7.35, 22°C
0.2
N-[5-[(1,3-benzodioxol-5-ylmethyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Haemophilus influenzae;
-
above, pH 7.35, 22°C
0.2
N-[5-[(1,3-benzodioxol-5-ylmethyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[5-[(1,3-benzodioxol-5-ylmethyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.004
N-[5-[(2-bromobenzyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli;
-
pH 7.35, 22°C
0.02
N-[5-[(2-bromobenzyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Haemophilus influenzae;
-
pH 7.35, 22°C
0.2
N-[5-[(2-bromobenzyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[5-[(2-bromobenzyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.005
N-[5-[(2-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli;
-
pH 7.35, 22°C
0.01
N-[5-[(2-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Haemophilus influenzae;
-
pH 7.35, 22°C
0.2
N-[5-[(2-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[5-[(2-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.015
N-[5-[(3-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli;
-
pH 7.35, 22°C
0.03
N-[5-[(3-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Haemophilus influenzae;
-
pH 7.35, 22°C
0.2
N-[5-[(3-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[5-[(3-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.025
N-[5-[(4-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli;
-
pH 7.35, 22°C
0.06
N-[5-[(4-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Haemophilus influenzae;
-
pH 7.35, 22°C
0.2
N-[5-[(4-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[5-[(4-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.13
N-[5-[butyl(propan-2-yl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli;
-
pH 7.35, 22°C
0.2
N-[5-[butyl(propan-2-yl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Haemophilus influenzae;
-
above, pH 7.35, 22°C
0.2
N-[5-[butyl(propan-2-yl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[5-[butyl(propan-2-yl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.015
N-[5-[ethyl(2-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli;
-
pH 7.35, 22°C
0.08
N-[5-[ethyl(2-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Haemophilus influenzae;
-
pH 7.35, 22°C
0.2
N-[5-[ethyl(2-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
N-[5-[ethyl(2-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
0.0002
[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]acetic acid
Escherichia coli;
-
pH 7.35, 22°C
0.0003
[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]acetic acid
Haemophilus influenzae;
-
pH 7.35, 22°C
0.2
[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]acetic acid
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.0001
[[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl]sulfanyl]acetic acid
Escherichia coli;
-
pH 7.35, 22°C
0.0002
[[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl]sulfanyl]acetic acid
Haemophilus influenzae;
-
pH 7.35, 22°C
0.2
[[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl]sulfanyl]acetic acid
Staphylococcus aureus;
-
above, pH 7.35, 22°C
0.2
[[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl]sulfanyl]acetic acid
Streptococcus pneumoniae;
-
above, pH 7.35, 22°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 8
-
alpha-D-galactosamine 1-phosphate substrate, pH 7.5, 80°C, recombinant mutant D005 protein
29.6
-
alpha-D-galactosamine 1-phosphate aubstrate, pH 7.5, 80°C, recombinant mutant D011 protein
47.6
-
alpha-D-galactosamine 1-phosphate aubstrate, pH 7.5, 80°C, recombinant wild-type ST0452 protein
67.4
-
alpha-D-glucosamine 1-phosphate substrate, pH 7.5, 80°C, recombinant wild-type ST0452 protein
75.34
-
pH 7.5, 80°C, substrates: acetyl-CoA + alpha-D-glucosamine 1-phosphate
323.5
-
alpha-D-glucosamine 1-phosphate substrate, pH 7.5, 80°C, recombinant mutant D005 protein
1131