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Target intelligence / Profile preview
Methionine Aminopeptidase (MetAP)
- Target
- MetAP
- Molecular classification
- Enzyme, Metalloprotease, Peptidase
01
Overview
Methionine aminopeptidase (MetAP) is a metalloprotease enzyme that catalyzes the removal of the N-terminal methionine from newly synthesized proteins. It exists in multiple isoforms (e.g., MetAP1 and MetAP2 in humans) and plays a critical role in protein maturation and various cellular processes, including cell cycle progression and angiogenesis. As such, it represents a promising target for anticancer therapy, with inhibitors being developed to block tumor growth and proliferation.
- Other names
- Methionyl aminopeptidasePeptidase ML-methionine aminopeptidaseMAP
02
Mechanism of action
Inhibition of MetAP activity leading to cell cycle arrest and/or anti-angiogenic effects
03
Biological functions
Protein maturationN-terminal methionine removalCell cycle regulationAngiogenesis regulation
04
Disease associations
Cancer
05
Safety considerations
Potential for off-target effects due to structural similarities with other metalloproteasesIsoform selectivity challenges in drug development
06
Interacting drugs
Fumagillin analogues
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