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Literature summary extracted from

  • Sink, R.; Kovac, A.; Tomasi?, T.; Rupnik, V.; Boniface, A.; Bostock, J.; Chopra, I.; Blanot, D.; Masic, L.P.; Gobec, S.; Zega, A.
    Synthesis and biological evaluation of N-acylhydrazones as inhibitors of MurC and MurD ligases (2008), ChemMedChem, 3, 1362-1370.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.2.8 MurC, overexpression in Escherichia coli strain JM83 Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.2.8 1H-indazole-3-carbohydrazide
-
 Escherichia coli
6.3.2.8 2-(4-{[(E)-2-(1H-indazol-3-ylcarbonyl)hydrazono]methyl} phenoxy) acetic acid complete inhibition at 0.5 mM Escherichia coli
6.3.2.8 2-phenyl-1,3-thiazole-5-carbohydrazide
-
 Escherichia coli
6.3.2.8 2-phenyl-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-1,3-thiazole-5-carbohydrazide 18% inhibition at 0.25 mM Escherichia coli
6.3.2.8 2-[4-({(E)-2-[(4-methyl-1,3-thiazol-5-yl)carbonyl]hydrazono} methyl)phenoxy]acetic acid complete inhibition at 0.5 mM Escherichia coli
6.3.2.8 4-({(E)-2-[(4-methyl-1,3-thiazol-5-yl)carbonyl]hydrazono} methyl)benzoic acid 94% inhibition at 0.5 mM Escherichia coli
6.3.2.8 4-methyl-1,3-thiazole-5-carbohydrazide
-
 Escherichia coli
6.3.2.8 4-methyl-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-1,3-thiazole-5-carbohydrazide 26% inhibition at 0.5 mM Escherichia coli
6.3.2.8 4-methyl-N'-[(E)-(2-phenyl-1,3-thiazol-4-yl)methylidene]-1,3-thiazole-5-carbohydrazide complete inhibition at 0.5 mM Escherichia coli
6.3.2.8 4-{[(E)-2-(1H-indazol-3-ylcarbonyl)hydrazono]methyl}benzoic acid complete inhibition at 0.5 mM Escherichia coli
6.3.2.8 benzohydrazide
-
 Escherichia coli
6.3.2.8 methyl4-({(E)-2-[(4-methyl-1,3-thiazol-5-yl)carbonyl]hydrazono}methyl)benzoate 95% inhibition at 0.5 mM Escherichia coli
6.3.2.8 methyl4-{[(E)-2-(1H-indazol-3-ylcarbonyl)hydrazono]methyl} benzoate complete inhibition at 0.5 mM Escherichia coli
6.3.2.8 additional information inhibitor design and synthesis, mass spectrometric analysis, ligand molecular docking calculations, inhibitory potency, MIC values lay above 0.128 mg/ml, overview Escherichia coli
6.3.2.8 N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-1H-indazole-3-carbohydrazide 42% inhibition at 0.25 mM Escherichia coli
6.3.2.8 N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide 64% inhibition at 0.10 mM Escherichia coli
6.3.2.8 N'-[(E)-(2,4-dihydroxyphenyl)methylidene]-1H-indazole-3-carbohydrazide 74% inhibition at 0.25 mM Escherichia coli
6.3.2.8 N'-[(E)-(2-hydroxyphenyl)methylidene]-1H-indazole-3-carbohydrazide complete inhibition at 0.25 mM Escherichia coli
6.3.2.8 N'-[(E)-(2-phenyl-1,3-thiazol-4-yl)methylidene]-1H-indazole-3-carbohydrazide 78% inhibition at 0.10 mM Escherichia coli
6.3.2.8 N'-[(E)-(2-phenyl-1,3-thiazol-4-yl)methylidene]benzohydrazide 70% inhibition at 0.25 mM Escherichia coli
6.3.2.8 N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-1H-indazole-3-carbohydrazide 36% inhibition at 0.5 mM Escherichia coli
6.3.2.8 N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-1,3-thiazole-5-carbohydrazide 95% inhibition at 0.5 mM Escherichia coli
6.3.2.8 N'-[(E)-(3,4-dihydroxyphenyl)methylidene]benzohydrazide complete inhibition at 0.5 mM Escherichia coli
6.3.2.8 N'-[(E)-(3,4-dimethoxyphenyl)methylidene]-1H-indazole-3-carbohydrazide complete inhibition at 0.5 mM Escherichia coli
6.3.2.8 N'-[(E)-(3,4-dimethoxyphenyl)methylidene]-4-methyl-1,3-thiazole-5-carbohydrazide complete inhibition at 0.5 mM Escherichia coli
6.3.2.8 N'-[(E)-(3,4-dimethoxyphenyl)methylidene]benzohydrazide 97% inhibition at 0.5 mM Escherichia coli
6.3.2.8 N'-[(E)-(3,5-dichloro-2-hydroxyphenyl)methylidene]-4-methyl-1,3-thiazole-5-carbohydrazide 43% inhibition at 0.25 mM Escherichia coli
6.3.2.8 N'-[(E)-(3-hydroxy-4-methoxyphenyl)methylidene] benzohydrazide 92% inhibition at 0.5 mM Escherichia coli
6.3.2.8 N'-[(E)-(3-hydroxy-4-methoxyphenyl)methylidene]-1H-indazole-3-carbohydrazide 67% inhibition at 0.25 mM Escherichia coli
6.3.2.8 N'-[(E)-(4-cyanophenyl)methylidene]-1H-indazole-3-carbohydrazide complete inhibition at 0.25 mM Escherichia coli
6.3.2.8 N'-[(E)-(4-cyanophenyl)methylidene]benzohydrazide complete inhibition at 0.25 mM Escherichia coli
6.3.2.8 N'-[(E)-(4-nitrophenyl)methylidene]-1H-indazole-3-carbohydrazide 91% inhibition at 0.5 mM Escherichia coli
6.3.2.8 N'-[(E)-1H-indol-3-ylmethylidene]-1H-indazole-3-carbohydrazide complete inhibition at 010 mM Escherichia coli
6.3.2.8 N'-[(E)-1H-indol-3-ylmethylidene]benzohydrazide 93% inhibition at 0.5 mM Escherichia coli
6.3.2.8 N'-{(E)-[4-(dimethylamino)phenyl]methylidene}-1H-indazole-3-carbohydrazide 95% inhibition at 0.25 mM Escherichia coli
6.3.2.8 N'-{(E)-[4-(dimethylamino)phenyl]methylidene}-4-methyl-1,3-thiazole-5-carbohydrazide 97% inhibition at 0.25 mM Escherichia coli
6.3.2.8 N'-{(E)-[4-(dimethylamino)phenyl]methylidene}benzohydrazide complete inhibition at 0.25 mM Escherichia coli
6.3.2.8 N-[(E)-(2,4-dihydroxyphenyl)methylidene]benzohydrazide complete inhibition at 0.5 mM Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.2.8 Mg2+
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.2.8 ATP + UDP-N-acetylmuramate + L-alanine Escherichia coli
-
 ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine
-
 ?
6.3.2.8 additional information Escherichia coli the Mur ligases constitute a series of four ATP-dependent enzymes, MurC to Mur, that are responsible for the stepwise addition of the pentapeptide side chain onto the D-lactoyl group of the uridine diphosphate-N-acetylmuramic acid initially formed via MurA and MurB, MurC catalyzes the additon of the first amino acid L-alanine. All of the Mur ligases catalyze the formation of an amide or peptide bond through the same reaction mechanism via a tetrahedral intermediate, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.8 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.2.8 recombinant MurC from Escherichia coli strain JM83 by anion exchange chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.8 ATP + UDP-N-acetylmuramate + L-alanine
-
 Escherichia coli ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine
-
 ?
6.3.2.8 additional information the Mur ligases constitute a series of four ATP-dependent enzymes, MurC to Mur, that are responsible for the stepwise addition of the pentapeptide side chain onto the D-lactoyl group of the uridine diphosphate-N-acetylmuramic acid initially formed via MurA and MurB, MurC catalyzes the additon of the first amino acid L-alanine. All of the Mur ligases catalyze the formation of an amide or peptide bond through the same reaction mechanism via a tetrahedral intermediate, overview Escherichia coli ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.3.2.8 MurC
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.2.8 37
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.2.8 8
-
 malachite green assay at Escherichia coli
6.3.2.8 8.6
-
 radioactive assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.2.8 ATP
-
 Escherichia coli

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
6.3.2.8 0.032
-
 pH 8.0, 37°C Escherichia coli 2-phenyl-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-1,3-thiazole-5-carbohydrazide
6.3.2.8 0.123
-
 pH 8.0, 37°C Escherichia coli 1H-indazole-3-carbohydrazide