Aminopeptidase puromycin-sensitive (NPEPPS)

Aminopeptidase puromycin-sensitive (NPEPPS) is a zinc-dependent metallopeptidase that cleaves amino acids from the N-terminus of peptides and proteins, displaying broad substrate specificity[1][3][4][6]. It is highly expressed in the cytoplasm of many tissues, including neural tissues, and is involved in degrading neuropeptides such as enkaphalins, processing polyglutamine peptides, and regulating protein turnover in the brain[1][3][4][6]. It also plays a critical role in the antigen-processing pathway for MHC class I molecules, as it contributes to the N-terminal trimming of peptide precursors presented to cytotoxic T cells[1][3]. This enzyme is implicated in several biological processes, including neuronal function, immune response, and cell cycle regulation. It has been associated with neurodegenerative conditions such as tauopathies (potentially Alzheimer's disease) due0to its efficiency in degrading tau protein, as well as with autism spectrum disorder[1]. NPEPPS is classified as a therapeutic target, with selective inhibitors (such as tosedostat) being explored for therapeutic intervention in various diseases[3].

Other names

Puromycin-sensitive aminopeptidasePSAAAP-SMP100Cytosol alanyl aminopeptidaseMetalloproteinase MP100

Inhibition of enzymatic (aminopeptidase) activity (as with tosedostat)[3]