thumb | right | alt=Leaf of a Drosera peltata with a captured ant. Royal National Park, NSW Australia, August 2011. | Leaf of a Drosera peltata with a captured ant. Royal National Park, NSW Australia, 2011. Nepenthesin (also spelled nepenthacin or nepenthasin) is an aspartic protease of plant origin that has so far been identified in the pitcher secretions of Nepenthes and in the leaves of Drosera peltata. It is similar to pepsin, but differs in that it also cleaves on either side of Asp residues and at Lys┼Arg. While more pH and temperature stable than porcine pepsin A, it is considerably le
thumb | right | alt=Leaf of a Drosera peltata with a captured ant. Royal National Park, NSW Australia, August 2011. | Leaf of a Drosera peltata with a captured ant. Royal National Park, NSW Australia, 2011. Nepenthesin (also spelled nepenthacin or nepenthasin) is an aspartic protease of plant origin that has so far been identified in the pitcher secretions of Nepenthes and in the leaves of Drosera peltata. It is similar to pepsin, but differs in that it also cleaves on either side of Asp residues and at Lys┼Arg. While more pH and temperature stable than porcine pepsin A, it is considerably less stable in urea or guanidine hydrochloride. It is the only known protein with such a stability profile.
The name nepenthesin was coined in 1968 by Shigeru Nakayama and Shizuko Amagase. Alternative names for this enzyme include '''Nepenthes acid proteinase and Nepenthes aspartic proteinase'. Two isozymes have been identified in Nepenthes: nepenthesin I and nepenthesin II. The production of large quantities of nepenthesin-1 through heterologous expression in Escherichia coli was described in 2014.
Discovered by embedding cosine similarity (sentence-transformers MiniLM, 384-dim).