Methionine aminopeptidase from Staphylococcus aureus (MetAP)

Methionine aminopeptidase from Staphylococcus aureus is an essential metalloenzyme responsible for the removal of N-terminal methionine from newly synthesized proteins, a crucial step in bacterial protein maturation. It acts as a dinuclear metalloprotease and typically functions as a mononuclear Fe2+-metalloprotease under physiological conditions. This enzyme’s activity is indispensable for bacterial life and virulence, making it a promising antibacterial drug target. Structural studies have led to potent inhibitors that target this enzyme specifically, and differences between bacterial and mammalian homologs have enabled efforts to develop selective antibacterial therapies.

Other names

Methionyl aminopeptidaseMAPStaphylococcus aureus MetAP

Direct inhibition of the enzyme’s active site, usually by the formation of a stable transition-state analogue (uncleavable tetrahedral intermediates mimic amide bond hydrolysis and block function)