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ATP + 1-phospho-N-acetylmuramoyl-L-Ala + Glu
ADP + phosphate + 1-phospho-N-acetylmuramoyl-L-Ala-D-Glu
-
-
-
-
?
ATP + dihydrouridine 5'-diphosphate-N-acetylmuramoyl-L-Ala + Glu
ADP + phosphate + dihydrouridine 5'-diphosphate-N-acetylmuramoyl-L-Ala-D-Glu
-
-
-
-
?
ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanine + D-glutamate
ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
ATP + UDP-N-acetylmuramate-L-alanine
adenosine 5'-tetraphosphate
ATP + UDP-N-acetylmuramate-L-alanine + D-glutamate
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
ATP + UDP-N-acetylmuramoyl-L-Ala + (+/-)trans-1-amino-3-carboxy-cyclohexanecarboxylic acid
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-(+/-)trans-1-amino-3-carboxy-cyclohexanecarboxylic acid
-
-
-
-
?
ATP + UDP-N-acetylmuramoyl-L-Ala + (+/-)trans-1-amino-3-carboxy-cyclopentanecarboxylic acid
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-(+/-)trans-1-amino-3-carboxy-cyclopentanecarboxylic acid
-
-
-
-
?
ATP + UDP-N-acetylmuramoyl-L-Ala + alpha-methyl-DL-Glu
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-alpha-methyl-DL-Glu
-
-
-
?
ATP + UDP-N-acetylmuramoyl-L-Ala + D-erythro-3-methylglutamic acid
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-erythro-3-methylglutamic acid
-
-
-
-
?
ATP + UDP-N-acetylmuramoyl-L-Ala + D-erythro-4-methylglutamic acid
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-erythro-4-methylglutamic acid
-
-
-
-
?
ATP + UDP-N-acetylmuramoyl-L-Ala + D-Glu
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu
-
-
-
-
?
ATP + UDP-N-acetylmuramoyl-L-Ala + DL-homocysteic acid
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-DL-homocysteic acid
-
-
-
-
?
ATP + UDP-N-acetylmuramoyl-L-Ala + Glu
?
ATP + UDP-N-acetylmuramoyl-L-Ala + Glu
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu
ATP + UDP-N-acetylmuramyl-L-alanine + D-glutamate
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
additional information
?
-
ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanine + D-glutamate
ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
-
-
-
?
ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanine + D-glutamate
ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
-
ATP in form of MgATP2-
-
-
?
ATP + UDP-N-acetylmuramate-L-alanine
adenosine 5'-tetraphosphate
-
-
-
?
ATP + UDP-N-acetylmuramate-L-alanine
adenosine 5'-tetraphosphate
-
-
-
?
ATP + UDP-N-acetylmuramate-L-alanine
adenosine 5'-tetraphosphate
-
-
-
?
ATP + UDP-N-acetylmuramate-L-alanine + D-glutamate
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
-
-
-
-
?
ATP + UDP-N-acetylmuramate-L-alanine + D-glutamate
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
-
-
-
r
ATP + UDP-N-acetylmuramate-L-alanine + D-glutamate
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
-
-
-
?
ATP + UDP-N-acetylmuramate-L-alanine + D-glutamate
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
-
-
-
r
ATP + UDP-N-acetylmuramoyl-L-Ala + Glu
?
-
key role in peptidoglycan biosynthesis
-
-
?
ATP + UDP-N-acetylmuramoyl-L-Ala + Glu
?
key role in peptidoglycan biosynthesis
-
-
?
ATP + UDP-N-acetylmuramoyl-L-Ala + Glu
?
-
activity is not in excess in the cell under normal growth conditions, but its amount is adjusted to the requirements of peptidoglycan synthesis
-
-
?
ATP + UDP-N-acetylmuramoyl-L-Ala + Glu
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu
-
-
-
-
?
ATP + UDP-N-acetylmuramoyl-L-Ala + Glu
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu
-
-
-
-
?
ATP + UDP-N-acetylmuramoyl-L-Ala + Glu
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu
-
-
-
-
?
ATP + UDP-N-acetylmuramoyl-L-Ala + Glu
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu
-
-
-
?
ATP + UDP-N-acetylmuramoyl-L-Ala + Glu
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu
highly stereospecific for D-Glu
-
-
?
ATP + UDP-N-acetylmuramoyl-L-Ala + Glu
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu
-
-
-
-
?
ATP + UDP-N-acetylmuramoyl-L-Ala + Glu
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu
-
-
-
-
?
ATP + UDP-N-acetylmuramoyl-L-Ala + Glu
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu
-
r
-
-
?
ATP + UDP-N-acetylmuramoyl-L-Ala + Glu
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu
-
DL -glutamine
-
-
?
ATP + UDP-N-acetylmuramoyl-L-Ala + Glu
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu
-
-
-
-
?
ATP + UDP-N-acetylmuramyl-L-alanine + D-glutamate
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
-
-
-
-
?
ATP + UDP-N-acetylmuramyl-L-alanine + D-glutamate
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
-
MurD is essential for cytoplasmic bacterial cell wall biosynthesis
-
-
?
ATP + UDP-N-acetylmuramyl-L-alanine + D-glutamate
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
-
-
-
?
ATP + UDP-N-acetylmuramyl-L-alanine + D-glutamate
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
the ligase MurD is involved in the process of peptidoglycan biosynthesis by catalyzing the addition of D-glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine
-
-
?
ATP + UDP-N-acetylmuramyl-L-alanine + D-glutamate
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
-
-
-
?
ATP + UDP-N-acetylmuramyl-L-alanine + D-glutamate
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
the ligase MurD is involved in the process of peptidoglycan biosynthesis by catalyzing the addition of D-glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine
-
-
?
additional information
?
-
-
structure-function analysis by hybrid quantum mechanical/molecular mechanical replica path method, three possible reaction pathways via tetrahedral intermediate, overview
-
-
?
additional information
?
-
enzyme MurD catalyzes the addition of D-glutamic acid to UDP-MurNAc-L-Ala in the presence of ATP
-
-
?
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(2R)-2-[((3-[(Z)-(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]phenyl)carbonyl)amino]pentanedioic acid
-
(2R)-2-[((4-[(Z)-(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]phenyl)carbonyl)amino]pentanedioic acid
-
(2R)-2-[[(7-(2-ethoxy-2-oxoethoxy)naphthalen-2-yl)sulfonyl]amino]pentanedioic acid
NMR and molecular dynamics analysis
(2R)-2-[[(7-(3-phenylpropoxy)naphthalen-2-yl)sulfonyl]amino]pentanedioic acid
NMR and molecular dynamics analysis
(2R)-2-[[(7-(4-cyanobenzyloxy)naphthalen-2-yl)sulfonyl]amino]pentanedioic acid
(2R)-2-[[(7-benzyloxynaphthalen-2-yl)sulfonyl]amino]pentanedioic acid
calculation of binding free energies. Main driving force for binding are non-polar van der Waals-interactions
(2R)-2-[[(7-butoxynaphthalen-2-yl)sulfonyl]amino]pentanedioic acid
NMR and molecular dynamics analysis
(2R)-2-[[(7-pentoxynaphthalen-2-yl)sulfonyl]amino]pentanedioic acid
calculation of binding free energies. Main driving force for binding are non-polar van der Waals-interactions
(2S)-2-[((4-[(Z)-(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]phenyl)carbonyl)amino]pentanedioic acid
-
(R,Z)-2-(3-((1-carboxy-N-(4-((4-oxo-2-thioxothiazolidin-5-ylidene)-methyl)phenyl)formamido)methyl)benzamido)pentanedioic acid
-
(R,Z)-2-(3-((2-carboxy-N-(4-((4-oxo-2-thioxothiazolidin-5-ylidene)-methyl)phenyl)acetamido)methyl)benzamido)pentanedioic acid
in addition, weak activity against Gram-positive Staphylococcus aureus and Enterococcus faecalis
(R,Z)-2-(3-((3-carboxy-N-(4-((4-oxo-2-thioxothiazolidin-5-ylidene)-methyl)phenyl)propanamido)methyl)benzamido)pentanedioic acid
in addition, weak activity against Gram-positive Staphylococcus aureus and Enterococcus faecalis
(R,Z)-2-(3-((4-((2,4-dioxothiazolidin-5-ylidene)methyl)phenylamino)methyl)benzamido)pentanedioic acid
-
(R,Z)-2-(3-((4-((4-oxo-2-thioxothiazolidin-5-ylidene)methyl)phenylamino)methyl)benzamido)pentanedioic acid
-
1-phospho-N-acetylmuramoyl-L-Ala-D-Glu
-
-
2,3,4,5-tetrabromo-6-(3,6-dihydroxy-9H-xanthen-9-yl)benzoic acid
inhibitor identified by structure-based virtual screening
2,4,6-Trinitrobenzenesulfonic acid
-
-
2-((4-[(2S)-butan-2-ylamino]-6-(ethylamino)-1,3,5-triazin-2-yl)sulfanyl)-N-(2-chlorophenyl)acetamide
0.5 mM, 50% inhibition. Inhibitory to both MurC and MurD, ECs 6.3.2.8 and 6.3.2.9, respectively
2-([2-(2-naphthylsulfonyl)hydrazono)methyl]phenyl 2-nitrobenzenesulfonate
-
71% inhibition at 0.05 mM
2-([2-(2-naphthylsulfonyl)hydrazono)methyl]phenyl 3-nitrobenzenesulfonate
-
70% inhibition at 0.05 mM
2-([2-(2-naphthylsulfonyl)hydrazono)methyl]phenyl 4-nitrobenzenesulfonate
-
-
2-([2-(naphthalen-2-ylsulfonyl)hydrazono]methyl)phenyl 2-(benzo[d][1,3]dioxol-5-yl)acetate
-
49% inhibition at 0.10 mM
2-bromo-N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)benzamide
-
-
2-[([6-[(4-cyano-2-fluorobenzyl)oxy]naphthalen-2-yl]sulfonyl)amino]-5-hydroxybenzoic acid
-
2-[([6-[(4-cyano-2-fluorobenzyl)oxy]naphthalen-2-yl]sulfonyl)amino]benzene-1,4-dicarboxylic acid
-
3-([[(5-amino-1,3,4-thiadiazol-2-yl)sulfanyl]acetyl]amino)-4-methylbenzoic acid
-
-
3-bromo-N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)benzamide
-
-
4-([(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl)-6-(naphthalen-2-ylmethyl)-1,3,5-triazin-2-amine
0.5 mM, 33% inhibition. Inhibitory to both MurC and MurD, ECs 6.3.2.8 and 6.3.2.9, respectively
4-cyano-N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)benzamide
-
78% inhibition at 0.05 mM
4-[([6-[(4-cyano-2-fluorobenzyl)oxy]naphthalen-2-yl]sulfonyl)amino]benzene-1,3-dicarboxylic acid
-
4-[([6-[(4-cyano-2-fluorobenzyl)oxy]naphthalen-2-yl]sulfonyl)amino]cyclohexane-1,3-dicarboxylic acid
-
6-([(1,1-dioxidotetrahydrothiophen-3-yl)sulfanyl]methyl)-N-(2-phenylethyl)-1,3,5-triazine-2,4-diamine
0.25 mM, 11% inhibition. Inhibitory to both MurC and MurD, ECs 6.3.2.8 and 6.3.2.9, respectively
6-[(1-methyl-1H-imidazol-2-yl)sulfanyl]-N,N'-diphenyl-1,3,5-triazine-2,4-diamine
0.5 mM, 30% inhibition. Inhibitory to both MurC and MurD, ECs 6.3.2.8 and 6.3.2.9, respectively
benzylidene rhodanines
-
possess MurC inhibitory activity in the low micromolar range
-
beta,gamma-methyleneadenosine 5'-triphosphate
-
nonhydrolyzable ATP analogue
CPAHWPHPC
-
i.e. peptide MD-C7C_1, inhibits MurD
CSAWSNKFC
-
i.e. peptide MD-C7C_2, inhibits MurD
D-erythro-3-Methylglutamic acid
-
-
D-erythro-4-Methylglutamic acid
-
-
dihydrouridine 5'-diphosphate-N-acetylmuramoyl-L-Ala-D-Glu
-
-
DL-2-Amino-4-phosphonobutyric acid
-
-
DL-2-aminopimelic acid
-
-
HSSWYIQHFPPL
-
i.e. peptide MD-12, inhibits MurD
N'-((2-[(2-nitrobenzyl)oxy]phenyl)methylidene)-2-naphthalenesulfonohydrazide
-
-
N'-((2-[(3-nitrobenzyl)oxy]phenyl)methylidene)-2-naphthalenesulfonohydrazide
-
70% inhibition at 0.05 mM
N'-((2-[(4-cyanobenzyl)oxy]phenyl)methylidene)(2-fluorophenyl)methanesulfonohydrazide
-
39% inhibition at 0.10 mM
N'-((2-[(4-cyanobenzyl)oxy]phenyl)methylidene)(phenyl)methanesulfonohydrazide
-
58% inhibition at 0.10 mM
N'-((2-[(4-cyanobenzyl)oxy]phenyl)methylidene)-2-naphthalenesulfonohydrazide
-
-
N'-((2-[(4-cyanobenzyl)oxy]phenyl)methylidene)-2-nitrobenzenesulfonohydrazide
-
86% inhibition at 0.10 mM
N'-((2-[(4-cyanobenzyl)oxy]phenyl)methylidene)-3-nitrobenzenesulfonohydrazide
-
74% inhibition at 0.10 mM
N'-((2-[(4-cyanobenzyl)oxy]phenyl)methylidene)[4-(trifluoromethyl)phenyl]methanesulfonohydrazide
-
57% inhibition at 0.10 mM
N'-((3-[(3-nitrobenzyl)oxy]phenyl)methylidene)-2-naphthalenesulfonohydrazide
-
61% inhibition at 0.05 mM
N-(2-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-3,5-dinitrobenzamide
-
-
N-(2-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-4-nitrobenzamide
-
-
N-(3-[[(carboxyacetyl)[4-[(Z)-(2,4-dioxo-1,3-thiazolidin-5-ylidene)methyl]phenyl]amino]methyl]benzoyl)-D-glutamic acid
-
N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-2-naphthamide
-
19% inhibition at 0.01 mM
N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-2-nitrobenzamide
-
-
N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-3,5-dinitrobenzamide
-
78% inhibition at 0.10 mM
N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-4-nitrobenzamide
-
81% inhibition at 0.05 mM
N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)benzamide
-
56% inhibition at 0.10 mM
N-(6-butoxy-naphthalene-2-sulfonyl)-D-glutamic acid
competitive versus D-Glu, non-competitive versus ATP and UDP-N-acetylmuramoyl-L-Ala
N-(6-butoxy-naphthalene-2-sulfonyl)-L-glutamic acid
competitive versus D-Glu, non-competitive versus UDP-N-acetylmuramoyl-L-Ala
N-([(2S)-2-[(2-naphthylsulfonyl)amino]propyl]-sulfonyl)-D-glutamic acid
-
1 mM, 75% residual activity
N-([(2S)-2-[([1,1'-biphenyl]-4-yl-sulfonyl)amino]-propyl]sulfonyl)-D-glutamic acid
-
1 mM, 70% residual activity
N-[((2S)-2-[[(E)-3-(1,3-benzodioxol-5-yl)-2-propenoyl]amino]propyl)sulfonyl]-D-glutamic acid
-
1 mM, 80% residual activity
N-[2-fluoro-5-[([4-[(Z)-(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]phenyl]amino)methyl]benzoyl]-D-glutamic acid
-
N-[[(2S)-2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propyl]sulfonyl]-D-glutamic acid
-
1 mM, 74% residual activity
N-[[(2S)-2-([2-[2-(acetylamino)phenoxy]acetyl]-amino)propyl]sulfonyl]-D-glutamic acid
-
1 mM, 93% residual activity
N-[[2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-ethyl]sulfonyl]-D-glutamic acid
-
1 mM, 77% residual activity
Phosphinate
-
an analogue of UDP-N-acetylmuramoyl-dipeptide, the N-acetylmuramoyl moiety being replaced by a hexanoyl chain and the peptide bond between L-Ala and D-Glu by a tetrahedral phosphinate bond
potassium phosphate
-
highly dependent on, optimal concentration: 11-16 mM, inhibition above 20 mM, phosphate ion is responsible for inhibition
RPTHSPI
-
peptides are synthesized from consensus sequences to evaluate their inhibitory potential against the essential MurD enzyme. The C-7-C mers MurDp1 (RPTHSPI) gives a decrease of MurD ATPase activity with a significant IC50 value of 4 mM. The 12 mers MurDp2 (HLPTSSLFDTTG) inhibits MurD with an IC50 value of 15 mM indicating a weak inhibition. Both peptides show a correlation between an increase in concentration versus an increase in inhibition values
UDP-N-acetylmuramoyl-L-Ala-D-Glu
-
-
[1-[(6-Uridinediphospho)hexanamido]ethyl](2,4-dicarboxybutyl)phosphinate pentasodium salt
-
good inhibitor, closely resembles the tetrahedral intermediate that is presumed to form the ligation reaction
(2R)-2-[[(7-(4-cyanobenzyloxy)naphthalen-2-yl)sulfonyl]amino]pentanedioic acid
NMR and molecular dynamics analysis
(2R)-2-[[(7-(4-cyanobenzyloxy)naphthalen-2-yl)sulfonyl]amino]pentanedioic acid
calculation of binding free energies. Main driving force for binding are non-polar van der Waals-interactions
L-Glu
-
-
L-Glu
-
50 mM, product inhibition
additional information
-
synthesis and evaluation of a series of transition-state analog inhibitors
-
additional information
-
design of peptidomimetic lead compounds with the ultimate objective of small molecule chemotherapeutic development, affinity selection by immobilized MurD with addition of ATP in an attempt to achieve conformationally homogenous population of target enzymes, overview. No inhibition by peptide MD-C7C_3, i.e. CQSSPHMSC
-
additional information
-
design and synthesis of N-benzylidenesulfonohydrazide inhibitors of MurC as antibacterial agents
-
additional information
generation of MurD 3D models using crystal structures of PDB entries 1EEH and 2JFF as templates in Modeller9v7 and generation of an in-house library of 1,496 MurD inhibitor analogs. Virtual screening of the best-ranked compounds with pharmacokinetics property prediction has provided 17 MurD inhibitors for developing anti-leptospirosis drug targeting peptidoglycan biosynthesis pathway
-
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0.2
1-phospho-N-acetylmuramoyl-L-Ala
-
-
0.01
dihydrouridine 5'-diphosphate-N-acetylmuramoyl-L-Ala
-
-
0.0073
UDP-N-acetylmuramate-L-alanine
-
37°C
0.012 - 0.304
UDP-N-acetylmuramoyl L-alanine
0.16
UDP-N-acetylmuramoyl-Ala
-
-
0.0055 - 0.041
UDP-N-acetylmuramoyl-L-Ala
additional information
additional information
ordered kinetic mechanism
-
0.03
ATP
-
pH 9.4, 37°C, E157A mutant protein
0.085
ATP
-
pH 9.4, 37°C, E157K mutant protein
0.114
ATP
-
pH 9.4, 37°C, D35A mutant protein
0.129
ATP
-
pH 9.4, 37°C, K198F mutant protein
0.13
ATP
-
pH 9.4, 37°C, H183A mutant protein
0.135
ATP
-
pH 9.4, 37°C, K198A mutant protein
0.14
ATP
-
pH 9.4, 37°C, N268A mutant protein
0.144
ATP
-
pH 9.4, 37°C, Y194F mutant protein
0.153
ATP
-
pH 9.4, 37°C, H301A mutant protein
0.183
ATP
-
pH 9.4, 37°C, R425A mutant protein
0.328
ATP
-
pH 9.4, 37°C, K115A mutant protein
1.58
ATP
-
pH 9.4, 37°C, N271A mutant protein
2
ATP
-
pH 9.4, 37°C, R302A mutant protein
2.18
ATP
-
pH 9.4, 37°C, D317A mutant protein
0.055
D-Glu
-
-
0.13
D-Glu
-
pH 8.8, 37°C
0.044
D-glutamate
-
pH 9.4, 37°C, D317A mutant protein
0.053
D-glutamate
-
pH 9.4, 37°C, N271A mutant protein
0.053
D-glutamate
-
pH 9.4, 37°C, Y194F mutant protein
0.056
D-glutamate
-
pH 9.4, 37°C, E157K mutant protein
0.074
D-glutamate
-
pH 9.4, 37°C, R302A mutant protein
0.095
D-glutamate
-
pH 9.4, 37°C, D35A mutant protein
0.095
D-glutamate
-
pH 9.4, 37°C, H301A mutant protein
0.128
D-glutamate
-
pH 9.4, 37°C, K115A mutant protein
0.185
D-glutamate
-
pH 9.4, 37°C, K198A mutant protein
0.216
D-glutamate
-
pH 9.4, 37°C, K198F mutant protein
0.264
D-glutamate
-
pH 9.4, 37°C, N268A mutant protein
0.806
D-glutamate
-
pH 9.4, 37°C, H183A mutant protein
5.16
D-glutamate
-
pH 9.4, 37°C, R425A mutant protein
0.012
UDP-N-acetylmuramoyl L-alanine
-
pH 9.4, 37°C, N268A mutant protein
0.016
UDP-N-acetylmuramoyl L-alanine
-
pH 9.4, 37°C, N271A mutant protein
0.04
UDP-N-acetylmuramoyl L-alanine
-
pH 9.4, 37°C, H301A mutant protein
0.046
UDP-N-acetylmuramoyl L-alanine
-
pH 9.4, 37°C, K115A mutant protein
0.053
UDP-N-acetylmuramoyl L-alanine
-
pH 9.4, 37°C, R425A mutant protein
0.057
UDP-N-acetylmuramoyl L-alanine
-
pH 9.4, 37°C, D317A mutant protein
0.059
UDP-N-acetylmuramoyl L-alanine
-
pH 9.4, 37°C, H183A mutant protein
0.065
UDP-N-acetylmuramoyl L-alanine
-
pH 9.4, 37°C, R302A mutant protein
0.084
UDP-N-acetylmuramoyl L-alanine
-
pH 9.4, 37°C, D35A mutant protein
0.111
UDP-N-acetylmuramoyl L-alanine
-
pH 9.4, 37°C, Y194F mutant protein
0.12
UDP-N-acetylmuramoyl L-alanine
-
pH 9.4, 37°C, K198A mutant protein
0.14
UDP-N-acetylmuramoyl L-alanine
-
pH 9.4, 37°C, K198F mutant protein
0.218
UDP-N-acetylmuramoyl L-alanine
-
pH 9.4, 37°C, E157K mutant protein
0.304
UDP-N-acetylmuramoyl L-alanine
-
pH 9.4, 37°C, E157A mutant protein
0.0055
UDP-N-acetylmuramoyl-L-Ala
-
-
0.006
UDP-N-acetylmuramoyl-L-Ala
-
0.0075
UDP-N-acetylmuramoyl-L-Ala
-
-
0.03
UDP-N-acetylmuramoyl-L-Ala
-
-
0.041
UDP-N-acetylmuramoyl-L-Ala
-
pH 8.8, 37°C
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0.089
(2R)-2-[((3-[(Z)-(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]phenyl)carbonyl)amino]pentanedioic acid
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.045
(2R)-2-[((4-[(Z)-(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]phenyl)carbonyl)amino]pentanedioic acid
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.192
(2R)-2-[[(7-(2-ethoxy-2-oxoethoxy)naphthalen-2-yl)sulfonyl]amino]pentanedioic acid
Escherichia coli
-
0.132
(2R)-2-[[(7-(3-phenylpropoxy)naphthalen-2-yl)sulfonyl]amino]pentanedioic acid
Escherichia coli
-
0.105
(2R)-2-[[(7-(4-cyanobenzyloxy)naphthalen-2-yl)sulfonyl]amino]pentanedioic acid
Escherichia coli
-
0.239
(2R)-2-[[(7-benzyloxynaphthalen-2-yl)sulfonyl]amino]pentanedioic acid
Escherichia coli
-
0.18
(2R)-2-[[(7-butoxynaphthalen-2-yl)sulfonyl]amino]pentanedioic acid
Escherichia coli
-
0.17
(2R)-2-[[(7-pentoxynaphthalen-2-yl)sulfonyl]amino]pentanedioic acid
Escherichia coli
-
0.01
(2S)-2-[((4-[(Z)-(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]phenyl)carbonyl)amino]pentanedioic acid
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.005
(R,Z)-2-(3-((1-carboxy-N-(4-((4-oxo-2-thioxothiazolidin-5-ylidene)-methyl)phenyl)formamido)methyl)benzamido)pentanedioic acid
Escherichia coli
pH not specified in the publication, temperature not specified in the publication. Malachite green assay in presence of 0.01% Triton X-100
0.003
(R,Z)-2-(3-((2-carboxy-N-(4-((4-oxo-2-thioxothiazolidin-5-ylidene)-methyl)phenyl)acetamido)methyl)benzamido)pentanedioic acid
Escherichia coli
pH not specified in the publication, temperature not specified in the publication. Malachite green assay in presence of 0.01% Triton X-100
0.007
(R,Z)-2-(3-((3-carboxy-N-(4-((4-oxo-2-thioxothiazolidin-5-ylidene)-methyl)phenyl)propanamido)methyl)benzamido)pentanedioic acid
Escherichia coli
pH not specified in the publication, temperature not specified in the publication. Malachite green assay in presence of 0.01% Triton X-100
0.085
(R,Z)-2-(3-((4-((2,4-dioxothiazolidin-5-ylidene)methyl)phenylamino)methyl)benzamido)pentanedioic acid
Escherichia coli
pH 8.0, 37°C
0.045
(R,Z)-2-(3-((4-((4-oxo-2-thioxothiazolidin-5-ylidene)methyl)phenylamino)methyl)benzamido)pentanedioic acid
Escherichia coli
pH 8.0, 37°C
0.01
2,3,4,5-tetrabromo-6-(3,6-dihydroxy-9H-xanthen-9-yl)benzoic acid
Escherichia coli
pH 8.0, 37°C
0.074
2-([2-(2-naphthylsulfonyl)hydrazono)methyl]phenyl 4-nitrobenzenesulfonate
Escherichia coli
-
pH 8.0, 37°C
0.055
2-bromo-N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)benzamide
Escherichia coli
-
pH 8.0, 37°C
0.046
2-[([6-[(4-cyano-2-fluorobenzyl)oxy]naphthalen-2-yl]sulfonyl)amino]-5-hydroxybenzoic acid
Escherichia coli
pH 8.6, 37°C
0.038
2-[([6-[(4-cyano-2-fluorobenzyl)oxy]naphthalen-2-yl]sulfonyl)amino]benzene-1,4-dicarboxylic acid
Escherichia coli
pH 8.6, 37°C
0.105
3-([[(5-amino-1,3,4-thiadiazol-2-yl)sulfanyl]acetyl]amino)-4-methylbenzoic acid
Escherichia coli
-
37°C
0.03
3-bromo-N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)benzamide
Escherichia coli
-
pH 8.0, 37°C
0.0084
4-[([6-[(4-cyano-2-fluorobenzyl)oxy]naphthalen-2-yl]sulfonyl)amino]benzene-1,3-dicarboxylic acid
Escherichia coli
pH 8.6, 37°C
0.182
4-[([6-[(4-cyano-2-fluorobenzyl)oxy]naphthalen-2-yl]sulfonyl)amino]cyclohexane-1,3-dicarboxylic acid
Escherichia coli
pH 8.6, 37°C
0.177
beta,gamma-methyleneadenosine 5'-triphosphate
Escherichia coli
-
37°C
1.5
CPAHWPHPC
Escherichia coli
-
pH 8.0, 37°C
0.62
CSAWSNKFC
Escherichia coli
-
pH 8.0, 37°C
0.14
HSSWYIQHFPPL
Escherichia coli
-
pH 8.0, 37°C
0.07
N'-((2-[(2-nitrobenzyl)oxy]phenyl)methylidene)-2-naphthalenesulfonohydrazide
Escherichia coli
-
pH 8.0, 37°C
0.062
N'-((2-[(4-cyanobenzyl)oxy]phenyl)methylidene)-2-naphthalenesulfonohydrazide
Escherichia coli
-
pH 8.0, 37°C
0.015
N-(3-[[(carboxyacetyl)[4-[(Z)-(2,4-dioxo-1,3-thiazolidin-5-ylidene)methyl]phenyl]amino]methyl]benzoyl)-D-glutamic acid
Escherichia coli
pH not specified in the publication, temperature not specified in the publication. Malachite green assay in presence of 0.01% Triton X-100
0.045
N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-2-nitrobenzamide
Escherichia coli
-
pH 8.0, 37°C
0.28
N-(6-butoxy-naphthalene-2-sulfonyl)-D-glutamic acid
Escherichia coli
-
0.71
N-(6-butoxy-naphthalene-2-sulfonyl)-L-glutamic acid
Escherichia coli
-
0.252
N-[2-fluoro-5-[([4-[(Z)-(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]phenyl]amino)methyl]benzoyl]-D-glutamic acid
Escherichia coli
pH not specified in the publication, temperature not specified in the publication. Malachite green assay in presence of 0.01% Triton X-100
15
RPTHSPI
Pseudomonas aeruginosa
-
peptides are synthesized from consensus sequences to evaluate their inhibitory potential against the essential MurD enzyme. The C-7-C mers MurDp1 (RPTHSPI) gives a decrease of MurD ATPase activity with a significant IC50 value of 4 mM. The 12 mers MurDp2
additional information
additional information
Pseudomonas aeruginosa
-
peptides are synthesized from consensus sequences to evaluate their inhibitory potential against the essential MurD enzyme. The C-7-C mers MurDp1 gives a decrease of MurD ATPase activity with a significant IC50 value of 4 mM. The 12 mers MurDp2 inhibits MurD with an IC50 value of 15 mM
-
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Linnett, P.E.; Tipper, D.J.
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Lysinibacillus sphaericus, Lysinibacillus sphaericus 9602
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Conditional mutants of Staphylococcus aureus defective in cell wall precursor synthesis
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1972
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Enzymatic synthesis of the peptide in bacterial uridine nucleotides. I. Enzymatic addition of L-alanine, D-glutamic acid, and L-lysine
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1962
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1982
Escherichia coli
brenda
Michaud, C.; Blanot, D.; Flouret, B.; van Heijenoort, J.
Partial purification and specificity studies of the D-glutamate-adding and D-alanyl-D-alanine-adding enzymes from Escherichia coli K12
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1987
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152
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1982
Bacillus subtilis, Bacillus subtilis 168
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1964
Staphylococcus aureus
brenda
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Escherichia coli
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18
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1990
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brenda
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2
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1996
Escherichia coli
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61
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brenda
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16
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1997
Escherichia coli (P14900), Escherichia coli
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Over-production, purification and properties of the uridine diphosphate N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli
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202
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1991
Escherichia coli
brenda
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38
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1999
Escherichia coli, Escherichia coli DH5-alpha
brenda
Gegnas, L.D.; Waddell, S.T.; Chabin, R.M.; Reddy, S.; Wong, K.K.
Inhibitors of the bacterial cell wall biosynthesis enzyme MurD
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8
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1998
Escherichia coli
brenda
Bouhss, A.; Dementin, S.; van Heijenoort, J.; Parquet, C.; Blanot, D.
Formation of adenosine 5'-tetraphosphate from the acyl phosphate intermediate: a difference between the MurC and MurD synthetases of Escherichia coli
FEBS Lett.
453
15-19
1999
Escherichia coli, Escherichia coli JM83(pMLD58)
brenda
El-Sherbeini, M.; Geissler, W.M.; Pittman, J.; Yuan, X.; Wong, K.K.; Pompliano, D.L.
Cloning and expression of Staphylococcus aureus and Streptococcus pyogenes murD genes encoding uridine diphosphate N-acetylmuramoyl-L-alanine:D-glutamate ligases
Gene
210
117-125
1998
Staphylococcus pyogenes, Staphylococcus aureus (P0A091), Staphylococcus pyogenes MB4439
brenda
Bertrand, J.A.; Auger, G.; Martin, L.; Fanchon, E.; Blanot, D.; Le Beller, D.; van Heijenoort, J.; Dideberg, O.
Determination of the MurD mechanism through crystallographic analysis of enzyme complexes
J. Mol. Biol.
289
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1999
Escherichia coli (P14900), Escherichia coli JM83(pMLD58) (P14900)
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301
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2000
Escherichia coli (P14900), Escherichia coli
brenda
Bouhss, A.; Dementin, S.; Van Heijenoort, J.; Parquet, C.; Blanot, D.
MurC and MurD synthetases of peptidoglycan biosynthesis: borohydride trapping of acyl-phosphate intermediates
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354
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2002
Escherichia coli, Escherichia coli JM83(pMLD58)
brenda
Auger, G.; Martin, L.; Bertrand, J.; Ferrari, P.; Fanchon, E.; Vaganay, S.; Petillot, Y.; van Heijenoort, J.; Blanot, D.; Dideberg, O.
Large-scale preparation, purification, and crystallization of UDP-N-acetylmuramoyl-L-alanine: D-glutamate ligase from Escherichia coli
Protein Expr. Purif.
13
23-29
1998
Escherichia coli, Escherichia coli JM83(pMLD58)
brenda
Kotnik, M.; Humljan, J.; Contreras-Martel, C.; Oblak, M.; Kristan, K.; Herve, M.; Blanot, D.; Urleb, U.; Gobec, S.; Dessen, A.; Solmajer, T.
Structural and functional characterization of enantiomeric glutamic acid derivatives as potential transition state analogue inhibitors of MurD ligase
J. Mol. Biol.
370
107-115
2007
Escherichia coli (P14900)
brenda
Paradis-Bleau, C.; Beaumont, M.; Boudreault, L.; Lloyd, A.; Sanschagrin, F.; Bugg, T.D.; Levesque, R.C.
Selection of peptide inhibitors against the Pseudomonas aeruginosa MurD cell wall enzyme
Peptides
27
1693-1700
2006
Pseudomonas aeruginosa
brenda
Humljan, J.; Kotnik, M.; Boniface, A.; Solmajer, T.; Urleb, U.; Blanot, D.; Gobec, S.
A new approach towards peptidosulfonamides: synthesis of potential inhibitors of bacterial peptidoglycan biosynthesis enzymes MurD and MurE
Tetrahedron
62
10980-10988
2006
Escherichia coli
-
brenda
Thakur, M.; Chakraborti, P.K.
Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase, to transphosphorylate MurD, a ligase involved in the process of peptidoglycan biosynthesis
Biochem. J.
415
27-33
2008
Mycobacterium tuberculosis (A5U4I2), Mycobacterium tuberculosis H37Ra / ATCC 25177 (A5U4I2)
brenda
Bratkovic, T.; Lunder, M.; Urleb, U.; Strukelj, B.
Peptide inhibitors of MurD and MurE, essential enzymes of bacterial cell wall biosynthesis
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48
202-206
2008
Escherichia coli
brenda
Frlan, R.; Kovac, A.; Blanot, D.; Gobec, S.; Pecar, S.; Obreza, A.
Design and synthesis of novel N-benzylidenesulfonohydrazide inhibitors of MurC and MurD as potential antibacterial agents
Molecules
13
11-30
2008
Escherichia coli
brenda
Perdih, A.; Hodoscek, M.; Solmajer, T.
MurD ligase from E. coli: Tetrahedral intermediate formation study by hybrid quantum mechanical/molecular mechanical replica path method
Proteins
15
744-759
2008
Escherichia coli
brenda
Turk, S.; Kovac, A.; Boniface, A.; Bostock, J.M.; Chopra, I.; Blanot, D.; Gobec, S.
Discovery of new inhibitors of the bacterial peptidoglycan biosynthesis enzymes MurD and MurF by structure-based virtual screening
Bioorg. Med. Chem.
17
1884-1889
2009
Escherichia coli (P14900)
brenda
Kristan, K.; Kotnik, M.; Oblak, M.; Urleb, U.
New high-throughput fluorimetric assay for discovering inhibitors of UDP-N-acetylmuramyl-L-alanine: D-glutamate (MurD) ligase
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14
412-418
2009
Escherichia coli
brenda
Simcic, M.; Hodoscek, M.; Humljan, J.; Kristan, K.; Urleb, U.; Kocjan, D.; Grdadolnik, S.G.
NMR and molecular dynamics study of the binding mode of naphthalene-N-sulfonyl-D-glutamic acid derivatives: novel MurD ligase inhibitors
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52
2899-2908
2009
Escherichia coli (P14900)
brenda
Perdih, A.; Bren, U.; Solmajer, T.
Binding free energy calculations of N-sulphonyl-glutamic acid inhibitors of MurD ligase
J. Mol. Model.
15
983-996
2009
Escherichia coli (P14900)
brenda
Patin, D.; Boniface, A.; Kovac, A.; Herv, M.; Dementin, S.; Barreteau, H.; Mengin-Lecreulx, D.; Blanot, D.
Purification and biochemical characterization of Mur ligases from Staphylococcus aureus
Biochimie
92
1793-1800
2010
Staphylococcus aureus
brenda
Sosic, I.; Barreteau, H.; Simcic, M.; Sink, R.; Cesar, J.; Zega, A.; Grdadolnik, S.G.; Contreras-Martel, C.; Dessen, A.; Amoroso, A.; Joris, B.; Blanot, D.; Gobec, S.
Second-generation sulfonamide inhibitors of d-glutamic acid-adding enzyme: Activity optimisation with conformationally rigid analogues of D-glutamic acid
Eur. J. Med. Chem.
46
2880-2894
2011
Escherichia coli (P14900)
brenda
Tomasic, T.; Kovac, A.; Simcic, M.; Blanot, D.; Grdadolnik, S.G.; Gobec, S.; Kikelj, D.; Peterlin Masic, L.
Novel 2-thioxothiazolidin-4-one inhibitors of bacterial MurD ligase targeting D-Glu- and diphosphate-binding sites
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46
3964-3975
2011
Escherichia coli (P14900), Escherichia coli
brenda
Umamaheswari, A.; Pradhan, D.; Hemanthkumar, M.
Virtual screening for potential inhibitors of homology modeled Leptospira interrogans MurD ligase
J. Chem. Biol.
13
175-187
2010
Leptospira interrogans (Q8F7V4)
-
brenda
Zidar, N.; Tomasic, T.; Sink, R.; Rupnik, V.; Kovac, A.; Turk, S.; Patin, D.; Blanot, D.; Contreras Martel, C.; Dessen, A.; Mueller Premru, M.; Zega, A.; Gobec, S.; Peterlin Masic, L.; Kikelj, D.
Discovery of novel 5-benzylidenerhodanine and 5-benzylidenethiazolidine-2,4-dione inhibitors of MurD ligase
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53
6584-6594
2010
Escherichia coli (P14900), Escherichia coli
brenda
Tomasic, T.; Zidar, N.; Sink, R.; Kovac, A.; Blanot, D.; Contreras-Martel, C.; Dessen, A.; Muller-Premru, M.; Zega, A.; Gobec, S.; Kikelj, D.; Peterlin Masic, L.
Structure-based design of a new series of D-glutamic acid based inhibitors of bacterial UDP-N-acetylmuramoyl-l-alanine:d-glutamate ligase (MurD)
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54
4600-4610
2011
Escherichia coli (P14900), Escherichia coli
brenda
Tomasic, T.; Kovac, A.; Klebe, G.; Blanot, D.; Gobec, S.; Kikelj, D.; Masic, L.P.
Virtual screening for potential inhibitors of bacterial MurC and MurD ligases
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18
1063-1072
2012
Escherichia coli (P14900)
brenda
Sink, R.; Kotnik, M.; Zega, A.; Barreteau, H.; Gobec, S.; Blanot, D.; Dessen, A.; Contreras-Martel, C.
Crystallographic study of peptidoglycan biosynthesis enzyme MurD: domain movement revisited
PLoS ONE
11
e0152075
2016
Escherichia coli (P14900)
brenda