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Literature summary for 3.4.11.18 extracted from

  • Chai, S.C.; Ye, Q.Z.
    Metal-mediated inhibition is a viable approach for inhibiting cellular methionine aminopeptidase (2009), Bioorg. Med. Chem. Lett., 19, 6862-6864.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
drug development MetAP is a promising target for developing broad spectrum antibacterial agents Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
N-(quinolin-8-yl)methanesulfonamide a trimetalated enzyme, forms a complex with the enzyme, cuases bacterial growth inhibition of strains AS19, D22 and SM101 by targeting MetAP by recruitment of a third auxiliary metal, binding structure, overview Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates, required for enzyme inhibition by inhibitor 1, overview Escherichia coli
Co2+ activates, required for enzyme inhibition by inhibitor 1, overview Escherichia coli
Fe2+ activates, required for enzyme inhibition by inhibitor 1, overview Escherichia coli
Mg2+ activates, required for enzyme inhibition by inhibitor 1, overview Escherichia coli
Mn2+ activates, required for enzyme inhibition by inhibitor 1, overview Escherichia coli
additional information MetAP can be activated in vitro by a number of divalent metals Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
strains AS19, D22 and SM101
-

Synonyms

Synonyms Comment Organism
MetAP
-
Escherichia coli
methionine aminopeptidase
-
Escherichia coli

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
additional information
-
IC50 values for N-(quinolin-8-yl)methanesulfonamide with different metal ions, overview Escherichia coli additional information

General Information

General Information Comment Organism
physiological function methionine aminopeptidase plays an essential role for cell survival Escherichia coli