Nepenthesin
| Nepenthesin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.23.12 | ||||||||
| CAS no. | 9073-80-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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
- ^ Jentsch J (April 1972). "Enzymes from carnivorous plants (nepenthes). Isolation of the protease nepenthacin". FEBS Lett. 21 (3): 273–276. doi:10.1016/0014-5793(72)80181-9. PMID 11946525.
- ^ Jentsch J, Meierkord S, Hammer M (1989). "The enzymes from carnivorous plants (Nepenthes): Properties and characterization of the acid protease nepenthacin". Planta Medica. 55 (2): 227. doi:10.1055/s-2006-961979.
- ^ a b c EC 3.4.23.12 - Nepenthesin. Integrated Enzyme Database (IntEnz).
- ^ Amagase S, Nakayama S, Tsugita A (October 1969). "Acid protease in Nepenthes. II. Study on the specificity of nepenthesin". J. Biochem. 66 (4): 431–9. PMID 5354017.
- ^ Amagase S (July 1972). "Digestive enzymes in insectivorous plants. 3. Acid proteases in the genus Nepenthes and Drosera peltata". J. Biochem. 72 (1): 73–81. PMID 5069751.
- ^ Amagase S, Mori M, Nakayama S (September 1972). "Digestive enzymes in insectivorous plants. IV. Enzymatic digestion of insects by Nepenthes secretion and Drosera peltata extract: proteolytic and chitinolytic activities". J. Biochem. 72 (3): 765–7. PMID 4634982.
- ^ Tökés ZA, Woon WC, Chambers SM (March 1974). "Digestive enzymes secreted by the carnivorous plant Nepenthes macferlanei L". Planta. 119 (1): 39–46. doi:10.1007/BF00390820.
- ^ Athauda SB, Inoue H, Iwamatsu A, Takahashi K (1998). "Acid Proteinase from Nepenthes distillatoria (Badura)". In James, Michael (ed.). Aspartic proteinases: retroviral and cellular enzymes. New York: Plenum. pp. 453–458. ISBN 0-306-45809-8.
- ^ Takahashi K, Tanji M, Shibata C (2007). "Variations in the content and isozymic composition of nepenthesin in the pitcher fluids among Nepenthes species" (PDF). Carnivorous Plant Newsletter. 36 (3): 73–76.
- ^ a b Kubota K, Metoki Y, Athauda SB, Shibata C, Takahashi K (2010). "Stability Profiles of Nepenthesin in Urea and Guanidine Hydrochloride: Comparison with Porcine Pepsin A". Bioscience, Biotechnology, and Biochemistry. 74 (11): 2323–2326. doi:10.1271/bbb.100391.
- ^ Nakayama S, Amagase S (1968). "Acid Protease in Nepenthes: Partial Purification and Properties of the Enzyme". Proceedings of the Japan Academy. 44 (5): 358–362.
- ^ Athauda SB, Matsumoto K, Rajapakshe S, Kuribayashi M, Kojima M, Kubomura-Yoshida N, Iwamatsu A, Shibata C, Inoue H, Takahashi K (July 2004). "Enzymic and structural characterization of nepenthesin, a unique member of a novel subfamily of aspartic proteinases". Biochem. J. 381 (Pt 1): 295–306. doi:10.1042/BJ20031575. PMC 1133788. PMID 15035659.
- ^ Kadek A, Tretyachenko V, Mrazek H, Ivanova L, Halada P, Rey M, Schriemer DC, Man P (March 2014). "Expression and characterization of plant aspartic protease nepenthesin-1 from Nepenthes gracilis". Protein Expression and Purification. 95: 121–128. doi:10.1016/j.pep.2013.12.005.
- ^ Takahashi K, Nishii W, Shibata C (2012). "The digestive fluid of Drosera indica contains a cysteine endopeptidase ("droserain") similar to dionain from Dionaea muscipula". Carnivorous Plant Newsletter. 41 (4): 132–134.