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Literature summary for 3.4.11.18 extracted from

  • Lowther, W.T.; McMillen, D.A.; Orville, A.M.; Matthews, B.W.
    The anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase (1998), Proc. Natl. Acad. Sci. USA, 95, 12153-12157.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
medicine the modification of the active site residue His79 by the inhibitors fumagillin and ovalicin may prevent the action of the enzyme on proteins or peptides involved in angiogenesis. These compounds may be effective pharmacological agents against pathogenic and resistant forms of Escherichia coli and other microorganisms Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
fumagillin fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase Escherichia coli
ovalicin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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