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Literature summary for 3.4.11.18 extracted from

  • Schiffmann, R.; Neugebauer, A.; Klein, C.D.
    Metal-mediated inhibition of Escherichia coli methionine aminopeptidase: structure-activity relationships and development of a novel scoring function for metal-ligand interactions (2006), J. Med. Chem., 49, 511-522.
    View publication on PubMed
Search for more literature for 3.4.11.18

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with thiabendazole Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
1-(1H-benzimidazol-2-yl)thiourea Co(II)-form of enzyme, 50% inhibition at 0.0089 mM Escherichia coli
1-benzyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole Co(II)-form of enzyme, 50% inhibition at 0.00046 mM Escherichia coli
1-benzyl-2-pyridin-2-yl-1H-benzimidazole Co(II)-form of enzyme, 50% inhibition at 0.00099 mM Escherichia coli
1-methyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole Co(II)-form of enzyme, 50% inhibition at 0.00050 mM Escherichia coli
2-(1,3-thiazol-4-yl)-1H-benzimidazol-5-amine Co(II)-form of enzyme, 50% inhibition at 0.00339 mM Escherichia coli
2-(1,3-thiazol-4-yl)-1H-imidazo(4,5-c)pyridine Co(II)-form of enzyme, 50% inhibition at 0.00172 mM Escherichia coli
2-(1H-benzimidazol-2-ylamino)pyridin-3-ol Co(II)-form of enzyme, 50% inhibition at 0.00078 mM Escherichia coli
2-(3H-pyrrol-5-yl)-1H-imidazo(4,5-b)pyridine Co(II)-form of enzyme, 50% inhibition at 0.000078 mM Escherichia coli
2-pyridin-2-yl-1H-benzimidazol-5-amine Co(II)-form of enzyme, 50% inhibition at 0.0097 mM Escherichia coli
2-pyridin-2-yl-1H-benzimidazole-5-carbonitrile Co(II)-form of enzyme, 50% inhibition at 0.00043 mM Escherichia coli
2-pyridin-2-yl-1H-imidazo(4,5-b)pyrazine Co(II)-form of enzyme, 50% inhibition at 0.00024 mM Escherichia coli
2-pyridin-2-yl-1H-imidazo(4,5-b)pyridine Co(II)-form of enzyme, 50% inhibition at 0.00011 mM Escherichia coli
2-pyridin-2-yl-1H-imidazo(4,5-c)pyridine Co(II)-form of enzyme, 50% inhibition at 0.00055 mM Escherichia coli
5,6-dimethyl-2-pyridin-2-yl-1H-benzimidazole Co(II)-form of enzyme, 50% inhibition at 0.00243 mM Escherichia coli
5-chloro-2-(1,3-thiazol-4-yl)-1H-benzimidazole Co(II)-form of enzyme, 50% inhibition at 0.00515 mM Escherichia coli
5-chloro-2-pyridin-2-yl-1H-benzimidazole Co(II)-form of enzyme, 50% inhibition at 0.00169 mM Escherichia coli
5-fluoro-2-(1,3-thiazol-4-yl)-1H-benzimidazole Co(II)-form of enzyme, 50% inhibition at 0.00431 mM Escherichia coli
5-fluoro-2-pyridin-2-yl-1H-benzimidazole Co(II)-form of enzyme, 50% inhibition at 0.00151 mM Escherichia coli
5-methyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole Co(II)-form of enzyme, 50% inhibition at 0.00716 mM Escherichia coli
5-methyl-2-pyridin-2-yl-1H-benzimidazole Co(II)-form of enzyme, 50% inhibition at 0.00209 mM Escherichia coli
5-nitro-2-(1,3-thiazol-4-yl)-1H-benzimidazole Co(II)-form of enzyme, 50% inhibition at 0.00122 mM Escherichia coli
5-nitro-2-pyridin-2-yl-1H-benzimidazole Co(II)-form of enzyme, 50% inhibition at 0.00016 mM Escherichia coli
5-tert-butyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole Co(II)-form of enzyme, 50% inhibition at 0.00391 mM Escherichia coli
5-tert-butyl-2-pyridin-2-yl-1H-benzimidazole Co(II)-form of enzyme, 50% inhibition at 0.00260 mM Escherichia coli
6-(1H-benzimidazol-2-ylamino)pyridin-2-ol Co(II)-form of enzyme, 50% inhibition at 0.00134 mM Escherichia coli
8-pyridin-2-yl-7H-purine Co(II)-form of enzyme, 50% inhibition at 0.00038 mM Escherichia coli
fumagillin Co(II)-form of enzyme, 50% inhibition at 0.000915 mM Escherichia coli
additional information thiabendazole and its derivatives are potent inhibitors in vitro, but fail to inhibit in vivo because they bind as Co2+-complexes to H79, thus blocking the active site of enzyme. In the in vitro assay the metal ion concentration is considerably higher than under in vivo conditions Escherichia coli
N-1,3-thiazol-2-yl-1H-benzimidazol-2-amine Co(II)-form of enzyme, 50% inhibition at 0.00054 mM Escherichia coli
N-1,3-thiazol-2-ylpyridine-2-carboxamide Co(II)-form of enzyme, 50% inhibition at 0.000063 mM, binds to an additional Co2+ ion at the entrance of the active site Escherichia coli
N-pyrazin-2-yl-1H-benzimidazol-2-amine Co(II)-form of enzyme, 50% inhibition at 0.0046 mM Escherichia coli
N-pyridin-2-yl-1H-benzimidazol-2-amine Co(II)-form of enzyme, 50% inhibition at 0.00057 mM Escherichia coli
phenyl(2-(1,3-thiazol-4-yl)-1H-benzimidazol-5-yl)methanone Co(II)-form of enzyme, 50% inhibition at 0.00240 mM Escherichia coli
phenyl(2-pyridin-2-yl-1H-benzimidazol-5-yl)methanone Co(II)-form of enzyme, 50% inhibition at 0.00040 mM Escherichia coli
thiabendazole Co(II)-form of enzyme, 50% inhibition at 0.00047 mM, binds to an additional Co2+ ion at the entrance of the active site Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AE18
-
-

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0004
-
 thiabendazole pH 7.5, 37°C Escherichia coli