This group of metallopeptidases belong to the MEROPS peptidase family M8 (leishmanolysin family, clan MA(M)). The protein fold of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA. Leishmanolysin () is an enzyme found in eukaryotes including Leishmania and related parasitic protozoa []. The endopeptidase is the most abundant protein on the cell surface during the promastigote stage of the parasite, and is attached to the membrane by a glycosylphosphatidylinositol anchor []. In the amastigote form, the parasite lives in lysosomes of host macrophages, producing a form of the protease that has an acidic pH optimum []. This differs from most other metalloproteases and may be an adaptation to the environment in which the organism survives [].Tris entry also includes proteins from humans and other chordates, including Leishmanolysin-like peptidase or invadolysin []and Ciliated left-right organizer metallopeptidase, CIROP). CIROP plays a role in left-right patterning process [].
