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phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
-
-
-
r
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
-
-
-
-
r
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
the enzyme catalyzes the first step in the biosynthesis of the bacterial cell wall
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
i.e. UDP-N-acetyl-D-glucosamine-enolpyruvate
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
i.e. UDP-N-acetyl-D-glucosamine-enolpyruvate
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
substrate binding structure
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
enzyme catalyzes the first committed step in the biosynthesis of bacterial cell wall peptidoglycan
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
pathway for biosynthesis of UDP-N-acetylmuramic acid
-
-
?
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(hydroxymethyl)phosphonic acid
i.e. CID-21680357
1-tuliposide A
potent inhibitor
1-tuliposide B
potent inhibitor
2-(4-methylpiperazin-1-yl)-3,4-dihydronaphthalen-1(2H)-one
-
2-oxo-1,3-benzoxathiol-5-yl (3-chlorophenyl)carbamate
-
2-oxo-1,3-benzoxathiol-6-yl benzenesulfonate
-
2-oxo-1,3-benzoxathiol-6-yl methanesulfonate
-
2-[4-(2-hydroxyethyl)piperazin-1-yl]-3,4-dihydronaphthalen-1(2H)-one
-
2-[4-(2-hydroxyethyl)piperazin-1-yl]-6,7-dimethoxy-3,4-dihydronaphthalen-1(2H)-one
-
4,7-dichloro-5-hydroxy-1,3-benzoxathiol-2-one
-
5-(prop-2-en-1-yloxy)-1,3-benzoxathiol-2-one
-
5-bromo-2-oxo-1,3-benzoxathiol-6-yl phenyl carbonate
-
5-hydroxy-1,3-benzoxathiol-2-one
-
5-hydroxy-7-(4-methoxyphenyl)-1,3-benzoxathiol-2-one
-
5-hydroxynaphtho[1,2-d][1,3]oxathiol-2-one
-
6,7-dimethoxy-2-[4-(2-phenylethyl)piperazin-1-yl]-3,4-dihydronaphthalen-1(2H)-one
-
cnicin
sesquiterpene lactone. The enzyme catalyzes the formation of a covalent adduct between cnicin and substrate UDP-N-acetylglucosamine via an anti-Michael 1,3-addition of UDP-N-acetylglucosamine to an alpha,beta-unsaturated carbonyl function in cnicin thus forming a noncovalent suicide inhibitor
HESFWYLPHHQSY
competitive inhibition
oxalic acid
i.e. AB-00005001
oxamic acid
i.e. ZINC04658565
phosphonomycin
irreversible inactivation, requires the presence of UDP-GlcNAc
-
pyrazolopyrimidine
reversible inhibitor
RWJ-110192
reversible inhibitor
RWJ-140998
irreversible inhibitor
RWJ-3981
irreversible inhibitor
T6361
competitive inhibition
T6362
competitive inhibition
Tartronic acid
i.e. ZINC901335
terreic acid
irreversible inhibitor
UDP-N-acetylmuramic acid
-
(+)-6-tuliposide B
-
25% residual activity at 0.1 mM
(+)-tulipalin B
-
2.5% residual activity at 0.1 mM
(-)-tulipalin B
-
2.8% residual activity at 0.1 mM
(E)-3-fluorophosphoenolpyruvate
(Z)-3-fluorophosphoenolpyruvate
2-(4-methylpiperazin-1-yl)-3,4-dihydronaphthalen-1(2H)-one
-
-
2-bromo-5-[(Z)-2-bromo-2-nitroethenyl]furan
-
-
2-oxo-1,3-benzoxathiol-5-yl (3-chlorophenyl)carbamate
-
-
2-oxo-1,3-benzoxathiol-5-yl methylcarbamate
-
-
2-oxo-1,3-benzoxathiol-5-yl pyridine-4-carboxylate
-
-
2-oxo-1,3-benzoxathiol-6-yl 4-nitrobenzenesulfonate
-
-
2-oxo-1,3-benzoxathiol-6-yl benzenesulfonate
-
-
2-oxo-1,3-benzoxathiol-6-yl methanesulfonate
-
-
2-oxo-1,3-benzoxathiol-6-yl sulfamate
-
-
3-methylidenedihydrofuran-2(3H)-one
-
87% residual activity at 0.1 mM
4,7-dichloro-5-hydroxy-1,3-benzoxathiol-2-one
-
-
5,7-dibromo-6-hydroxy-1,3-benzoxathiol-2-one
-
-
5-(prop-2-en-1-yloxy)-1,3-benzoxathiol-2-one
-
-
5-hydroxy-7-(3-methylphenyl)-1,3-benzoxathiol-2-one
-
-
5-hydroxy-7-(4-methoxyphenyl)-1,3-benzoxathiol-2-one
-
-
5-hydroxybenzo[d][1,3]oxathiol-2-one
-
-
5-hydroxynaphtho[1,2-d][1,3]oxathiol-2-one
-
-
5-hydroxynaphtho[2,1-d][1,3]oxathiol-2-one
-
-
5-methoxy-1,3-benzoxathiole
-
-
5-methoxybenzo[d][1,3]oxathiol-2-one
-
-
7-(4-fluorophenyl)-5-hydroxy-1,3-benzoxathiol-2-one
-
-
7-chloro-6-(4-hydroxyphenoxy)quinoline-5,8-dione
-
-
Co2+
-
metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM
Cu2+
-
metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM
epi-(+)-6-tuliposide B
-
17% residual activity at 0.1 mM
Fe2+
-
metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM
HESFWYLPHHQSY
-
competitive inhibition
MnCl2
-
metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM
UDP-N-acetylmuramic acid-L-Ala
-
weak
UDP-N-acetylmuramic acid-L-Ala-D-Glu
-
weak
UDP-N-acetylmuramyl-L-Ala-D-Glu-meso-alpha,epsilon-diaminopimelic acid
-
above 1 mM
uridine diphospho-N-acetylmuramyl-L-Ala-D-gamma-Glu-meso-alpha,epsilon-diaminopimelic-acid-D-Ala-D-Ala
-
above 1 mM
Zn2+
-
metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM
fosfomycin
-
fosfomycin
irreversible inhibitor
fosfomycin
enolpyruvyl UDP-GlcNAc synthase is an antimicrobial target that is inhibited by the antibiotic fosfomycin
fosfomycin
acting competitively as an analogue of phosphoenolpyruvate
(E)-3-fluorophosphoenolpyruvate
-
inactivation
(E)-3-fluorophosphoenolpyruvate
-
kinetics
(E)-3-fluorophosphoenolpyruvate
-
pseudosubstrate, formation of a tetrahedral intermediate in the reaction pathway, investigation of chirality of the intermediate stereospecifically formed at the active site in D2O
(E)-3-fluorophosphoenolpyruvate
-
formation of 2 reaction intermediates: a covalent phosphofluorolactyl-enzyme adduct and a free phosphofluorolactyl-UDP-GlcNAc tetrahedral adduct
(Z)-3-fluorophosphoenolpyruvate
-
inactivation
(Z)-3-fluorophosphoenolpyruvate
-
kinetics
(Z)-3-fluorophosphoenolpyruvate
-
pseudosubstrate, formation of a tetrahedral intermediate in the reaction pathway, investigation of chirality of the intermediate stereospecifically formed at the active site in D2O
(Z)-3-fluorophosphoenolpyruvate
-
formation of 2 reaction intermediates: a covalent phosphofluorolactyl-enzyme adduct and a free phosphofluorolactyl-UDP-GlcNAc tetrahedral adduct
(Z)-3-fluorophosphoenolpyruvate
-
kinetics, mutant C115D
(Z)-3-fluorophosphoenolpyruvate
-
wild-type and mutant C115D, competitive against phosphoenolpyruvate
fosfomycin
-
-
fosfomycin
-
irreversible inhibition
fosfomycin
-
binding study by isothermal titration calorimetry
fosfomycin
-
binds covalently to Cys115
fosfomycin
-
competitive against phosphoenolpyruvate
fosfomycin
-
alkylates Cys115
fosfomycin
-
t1/2 for inactivation of the wild-type enzyme: 6 s
fosfomycin
-
inhibits the wild-type, mutant C155D is completely resistant
fosfomycin
-
selectively inhibited by fosfomycin, which forms a covalent bond to the sulfhydryl group of the catalytically relevant Cys115 residue
PGE-553828
-
competitive against UDP-GlcNAc
-
PGE-553828
-
inhibition mechanism, kinetics
-
phosphonomycin
-
inhibitor binding site is distinct from active site
-
phosphonomycin
-
i.e. L-cis-2-epoxypropylphosphonic acid
-
phosphonomycin
-
irreversible inactivation, requires the presence of UDP-GlcNAc
-
UDP-N-acetylmuramic acid
-
weak
UDP-N-acetylmuramic acid
-
competitive with phosphate
additional information
insight into the catalytic mechanism and covalent inhibition by QM/MM MD simulations
-
additional information
-
no inhibition by UDP-galactose
-
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0.00853
2-(4-methylpiperazin-1-yl)-3,4-dihydronaphthalen-1(2H)-one
Escherichia coli
-
0.02249
2-[4-(2-hydroxyethyl)piperazin-1-yl]-3,4-dihydronaphthalen-1(2H)-one
Escherichia coli
-
0.00313
2-[4-(2-hydroxyethyl)piperazin-1-yl]-6,7-dimethoxy-3,4-dihydronaphthalen-1(2H)-one
Escherichia coli
-
0.02256
6,7-dimethoxy-2-[4-(2-phenylethyl)piperazin-1-yl]-3,4-dihydronaphthalen-1(2H)-one
Escherichia coli
-
0.00046
fosfomycin
Escherichia coli
-
0.002
(+/-)-tulipaline B
Escherichia coli
-
pH and temperature not specified in the publication
0.00853
2-(4-methylpiperazin-1-yl)-3,4-dihydronaphthalen-1(2H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.0028
2-bromo-5-[(Z)-2-bromo-2-nitroethenyl]furan
Escherichia coli
-
pH and temperature not specified in the publication
0.00286
2-oxo-1,3-benzoxathiol-5-yl (3-chlorophenyl)carbamate
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00046
2-oxo-1,3-benzoxathiol-5-yl methylcarbamate
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00058
2-oxo-1,3-benzoxathiol-5-yl pyridine-4-carboxylate
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00515
2-oxo-1,3-benzoxathiol-6-yl 4-nitrobenzenesulfonate
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00196
2-oxo-1,3-benzoxathiol-6-yl benzenesulfonate
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00076
2-oxo-1,3-benzoxathiol-6-yl methanesulfonate
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00025 - 0.00243
2-oxo-1,3-benzoxathiol-6-yl sulfamate
0.00028
4,7-dichloro-5-hydroxy-1,3-benzoxathiol-2-one
0.00095
5,7-dibromo-6-hydroxy-1,3-benzoxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00801
5-(prop-2-en-1-yloxy)-1,3-benzoxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00727
5-hydroxy-7-(3-methylphenyl)-1,3-benzoxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00951
5-hydroxy-7-(4-methoxyphenyl)-1,3-benzoxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00053
5-hydroxybenzo[d][1,3]oxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.0031
5-hydroxynaphtho[1,2-d][1,3]oxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00155
5-hydroxynaphtho[2,1-d][1,3]oxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.01428
5-methoxy-1,3-benzoxathiole
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00645
5-methoxybenzo[d][1,3]oxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.01854
7-(4-fluorophenyl)-5-hydroxy-1,3-benzoxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.0103
cnicin
Escherichia coli
-
pH and temperature not specified in the publication
0.006
Cpd1
Escherichia coli
-
pH and temperature not specified in the publication
-
0.0006 - 0.0088
fosfomycin
0.0002
RWJ-3981
Escherichia coli
-
pH and temperature not specified in the publication
0.00025
2-oxo-1,3-benzoxathiol-6-yl sulfamate
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00243
2-oxo-1,3-benzoxathiol-6-yl sulfamate
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00028
4,7-dichloro-5-hydroxy-1,3-benzoxathiol-2-one
Escherichia coli
-
pH and temperature not specified in the publication
0.00028
4,7-dichloro-5-hydroxy-1,3-benzoxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.0006
fosfomycin
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00077
fosfomycin
Escherichia coli
-
enzyme is pre-incubated with the inhibitor in the presence of 1 mM UDP-N-acetyl-D-glucosamine, reaction is started by addition of phosphoenolpyruvate
0.0051
fosfomycin
Escherichia coli
-
enzyme shows 5-7fold shift in IC50 for the inhibitor upon pre-incubation with the substrate UDP-N-acetyl-D-glucosamine
0.0088
fosfomycin
Escherichia coli
-
pH and temperature not specified in the publication
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Venkateswaran, P.S.; Lugtenberg, E.J.J.; Wu, H.C.
Inhibition of phosphoenolpyruvate:uridine diphosphate N-acetylglucosamine enolpyruvyltransferase by uridine diphosphate N-acetylmuramyl peptides
Biochim. Biophys. Acta
293
570-574
1973
Bacillus cereus, Bacillus cereus T, Escherichia coli, Escherichia coli K-235
brenda
Marquardt, J.L.; Siegele, D.A.; Kolter, R.; Walsh, C.T.
Cloning and sequencing of Escherichia coli murZ and purification of its product, a UDP-N-acetylglucosamine enolpyruvyl transferase
J. Bacteriol.
174
5748-5752
1992
Escherichia coli (P0A749), Escherichia coli
brenda
Brown, E.D.; Vivas, E.I.; Walsh, C.T.; Kolter, R.
MurA (MurZ), the enzyme that catalyzes the first committed step in peptidoglycan biosynthesis, is essential in Escherichia coli
J. Bacteriol.
177
4194-4197
1995
Escherichia coli (P0A749), Escherichia coli
brenda
Kim, D.H.; Lees, W.J.; Walsh, C.T.
Stereochemical analysis of the tetrahedral adduct formed at the active site of UDP-GlcNAc enolpyruvyl transferase from the pseudosubstrates, (E)- and (Z)-3-fluorophosphoenolpyruvate, in D2O
J. Am. Chem. Soc.
117
6380-6381
1995
Escherichia coli, Escherichia coli MurZ
-
brenda
Kim, D.H.; Lees, W.J.; Haley, T.M.; Walsh, C.T.
Kinetic characterization of the inactivation of UDP-GlcNAc enolpyruvyl transferase by (Z)-3-fluorophosphoenolpyruvate: evidence for two oxocarbenium ion intermediates in enolpyruvyl transfer catalysis
J. Am. Chem. Soc.
117
1494-1502
1995
Escherichia coli, Escherichia coli MurZ
-
brenda
Kim, D.H.; Lees, W.J.; Kempsell, K.E.; Lane, W.S.; Duncan, K.; Walsh, C.T.
Characterization of a Cys115 to Asp substitution in the Escherichia coli cell wall biosynthetic enzyme UDP-GlcNAc enolpyruvyl transferase (MurA) that confers resistance to inactivation by the antibiotic fosfomycin
Biochemistry
35
4923-4928
1996
Enterobacter cloacae, Escherichia coli, Escherichia coli MurA
brenda
Skarzynski, T.; Mistry, A.; Wonacott, A.; Hutchinson, S.E.; Kelly, V.A.; Duncan, K.
Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, and enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin
Structure
4
1465-1474
1996
Escherichia coli
brenda
Dai, H.J.; Parker, C.N.; Bao, J.J.
Characterization and inhibition study of MurA enzyme by capillary electrophoresis
J. Chromatogr. B
766
123-132
2002
Escherichia coli, Escherichia coli MurA
brenda
Mizyed, S.; Oddone, A.; Byczynski, B.; Hughes, D.W.; Berti, P.J.
UDP-N-acetylmuramic acid (UDP-MurNAc) is a potent inhibitor of MurA (enolpyruvyl-UDP-GlcNAc synthase)
Biochemistry
44
4011-4017
2005
Escherichia coli
brenda
Byczynski, B.; Mizyed, S.; Berti, P.J.
Nonenzymatic breakdown of the tetrahedral (alpha-carboxyketal phosphate) intermediates of MurA and AroA, two carboxyvinyl transferases. Protonation of different functional groups controls the rate and fate of breakdown
J. Am. Chem. Soc.
125
12541-12550
2003
Escherichia coli
brenda
Zhang, F.; Berti, P.J.
Phosphate analogues as probes of the catalytic mechanisms of MurA and AroA, two carboxyvinyl transferases
Biochemistry
45
6027-6037
2006
Escherichia coli
brenda
Klein, C.D.; Bachelier, A.
Molecular modeling and bioinformatical analysis of the antibacterial target enzyme MurA from a drug design perspective
J. Comput. Aided Mol. Des.
20
621-628
2006
Enterobacter cloacae, Escherichia coli
brenda
Dunsmore, C.J.; Miller, K.; Blake, K.L.; Patching, S.G.; Henderson, P.J.; Garnett, J.A.; Stubbings, W.J.; Phillips, S.E.; Palestrant, D.J.; Angeles, J.D.; Leeds, J.A.; Chopra, I.; Fishwick, C.W.
2-Aminotetralones: novel inhibitors of MurA and MurZ
Bioorg. Med. Chem. Lett.
18
1730-1734
2008
Staphylococcus aureus, Escherichia coli (P0A749)
brenda
Steinbach, A.; Scheidig, A.J.; Klein, C.D.
The unusual binding mode of cnicin to the antibacterial target enzyme MurA revealed by X-ray crystallography
J. Med. Chem.
51
5143-5147
2008
Escherichia coli (P0A749)
brenda
Jackson, S.G.; Zhang, F.; Chindemi, P.; Junop, M.S.; Berti, P.J.
Evidence of kinetic control of ligand binding and staged product release in MurA (enolpyruvyl UDP-GlcNAc synthase)-catalyzed reactions
Biochemistry
48
11715-11723
2009
Escherichia coli (P0A749)
brenda
Dube, S.; Nanda, K.; Rani, R.; Kaur, N.; Nagpal, J.; Upadhyay, D.; Cliffe, I.; Saini, K.; Purnapatre, K.
UDP-N-acetylglucosamine enolpyruvyl transferase from Pseudomonas aeruginosa
World J. Microbiol. Biotechnol.
26
1623-1629
2010
Escherichia coli, Pseudomonas aeruginosa
brenda
Gautam, A.; Rishi, P.; Tewari, R.
UDP-N-acetylglucosamine enolpyruvyl transferase as a potential target for antibacterial chemotherapy: recent developments
Appl. Microbiol. Biotechnol.
92
211-225
2011
Enterobacter cloacae (P33038), Escherichia coli (P0A749), Mycobacterium tuberculosis (P9WJM1), Mycobacterium tuberculosis H37Rv (P9WJM1), Pseudomonas aeruginosa, Staphylococcus aureus, Streptococcus pneumoniae
brenda
Miller, K.; Dunsmore, C.J.; Leeds, J.A.; Patching, S.G.; Sachdeva, M.; Blake, K.L.; Stubbings, W.J.; Simmons, K.J.; Henderson, P.J.; De Los Angeles, J.; Fishwick, C.W.; Chopra, I.
Benzothioxalone derivatives as novel inhibitors of UDP-N-acetylglucosamine enolpyruvyl transferases (MurA and MurZ)
J. Antimicrob. Chemother.
65
2566-2573
2010
Escherichia coli, Escherichia coli JM109, Staphylococcus aureus, Staphylococcus aureus SH1000
brenda
Hrast, M.; Sosic, I.; Sink, R.; Gobec, S.
Inhibitors of the peptidoglycan biosynthesis enzymes MurA-F
Bioorg. Chem.
55
2-15
2014
Escherichia coli
brenda
Shigetomi, K.; Olesen, S.H.; Yang, Y.; Mitsuhashi, S.; Schoenbrunn, E.; Ubukata, M.
MurA as a primary target of tulipalin B and 6-tuliposide B
Biosci. Biotechnol. Biochem.
77
2517-2519
2013
Enterobacter cloacae, Escherichia coli
brenda
Boulhissa, I.; Chikhi, A.; Bensegueni, A.; Ghattas, M.A.; Mokrani, E.H.; Alrawashdeh, S.; Eddin Obaid, D.E.
Investigation for new inhibitors of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) by virtual screening with antibacterial sssessment
Curr. Comput. Aided Drug Des.
17
214-224
2020
Escherichia coli (P0A749), Escherichia coli, Escherichia coli K12 (P0A749)
brenda
Mihalovits, L.M.; Ferenczy, G.G.; Keseru, G.M.
Catalytic mechanism and covalent inhibition of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) Implications to the design of novel antibacterials
J. Chem. Inf. Model.
59
5161-5173
2019
Escherichia coli (P0A749)
brenda