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Nepenthesin
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.〔
The names cephalotusin, dionaeasin and droserasin have been proposed for similar aspartic endopeptidases originating from the carnivorous plant genera ''Cephalotus'', ''Dionaea'' and ''Drosera'', respectively.〔
==References==
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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