InterPro domain: IPR043577

This entry represents a group of asparagine-specific endopeptidases, including Legumain from mammals, Hemoglobinase from Schistosoma mansoni (Blood fluke) and Vacuolar-processing enzyme from plants.

Asparaginyl endopeptidase is a family of cysteine proteases found in many organisms. This group of cysteine peptidases belong to the MEROPS peptidase family C13 (legumain family, clan CD). A type example is legumain from Canavalia ensiformis (Jack bean, Horse bean) [ 1 ]. Although legumains were first described from beans (also known as Vacuolar Processing Enzymes), homologues have been identified in plants, protozoa, vertebrates, and helminths [ 2 , 3 ]. In blood-feeding helminths, asparaginyl endopeptidases (sometimes described as hemoglobinases) have been located in the gut and are considered to be involved in host hemoglobin digestion [ 4 , 5 , 6 , 7 ].

1. Isolation and analysis of cDNA encoding a precursor of Canavalia ensiformis asparaginyl endopeptidase (legumain). J. Biochem. 116, 541-6
2. Families of cysteine peptidases. Meth. Enzymol. 244, 461-86
3. Cloning, isolation, and characterization of mammalian legumain, an asparaginyl endopeptidase. J. Biol. Chem. 272, 8090-8
4. Expression and partial characterization of a cathepsin B-like enzyme (Sm31) and a proposed 'haemoglobinase' (Sm32) from Schistosoma mansoni. Biochem. J. 290 ( Pt 3), 801-6
5. Schistosome asparaginyl endopeptidase SM32 in hemoglobin digestion. Parasitol. Today (Regul. Ed.) 12, 125
6. Identification and characterization of an asparaginyl endopeptidase from Angiostrongylus cantonensis. Parasitol. Res. 113, 2143-52
7. A multienzyme network functions in intestinal protein digestion by a platyhelminth parasite. J. Biol. Chem. 281, 39316-29