Thimet oligopeptidase (THOP1)

Thimet oligopeptidase (THOP1) is a zinc-dependent metallopeptidase broadly distributed in mammalian tissues, with particularly high activity in the brain. THOP1 cleaves cytosolic peptides—usually from 5 to 22 amino acids in length, with preference for 9–12 amino acids—and inactivates neuropeptides such as bradykinin, gonadotropin-releasing hormone (GnRH), dynorphin A, and others. It is a key player in peptide metabolism, participates in the regulation of MHC class I antigen presentation, and modulates signaling by controlling the degradation of bioactive peptides. THOP1 has been implicated in neurological, metabolic, and immune-related processes. Its activity depends on metal ion cofactors (notably Zn^2+), and the enzyme displays high thiol-sensitivity due to cysteine content[1][2][4]. Dysregulated THOP1 activity has been associated with metabolic disease, altered immune responses, neurodegeneration, and pain. While no selective therapeutic agents are approved for THOP1, it remains a subject of biomedical research for its multiple biological and pathological roles[1][2][4].

Other names

Endopeptidase 24.15EP24.15MP78MEPD_HUMANTOPbrain kininase Akininase Aendo-oligopeptidase APz-peptidase

Inhibition of catalytic (metallopeptidase) activity, usually through zinc chelation or small molecule inhibitors Modulation of antigen processing and peptide degradation