Nepenthesin
| Nepenthesin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.23.12 | ||||||||
| CAS number | Template:CAS | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
|
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Nepenthesin (also spelled nepenthacin[1][2] or nepenthasin[3]) 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.[4][5][6][7][8][9] It is similar to pepsin, but differs in that it also cleaves on either side of Asp residues and at Lys┼Arg.[3] While more pH and temperature stable than porcine pepsin A, it is considerably less stable in urea or guanidine hydrochloride.[10] It is the only known protein with such a stability profile.[10]
The name nepenthesin was coined in 1968 by Shigeru Nakayama and Shizuko Amagase.[11] Alternative names for this enzyme include Nepenthes acid proteinase and Nepenthes aspartic proteinase.[3] Two isozymes have been identified in Nepenthes: nepenthesin I and nepenthesin II.[12] The production of large quantities of nepenthesin-1 through heterologous expression in Escherichia coli was described in 2014.[13]
The names cephalotusin, dionaeasin and droserasin have been proposed for similar aspartic endopeptidases originating from the carnivorous plant genera Cephalotus, Dionaea and Drosera, respectively.[14]
References
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- ↑ 3.0 3.1 3.2 EC 3.4.23.12 - Nepenthesin. Integrated Enzyme Database (IntEnz).
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- ↑ 10.0 10.1 Lua error in package.lua at line 80: module 'strict' not found.
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