Biology:Nepenthesin
| Nepenthesin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.23.12 | ||||||||
| CAS number | 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]
Discovery
In the late 19th century, Sydney Howard Vines showed that the pitcher fluid from Nepenthes could digest protein in acidic conditions. He suggested the plants were making a digestive enzyme, for which he proposed the name "nepenthin".[15] In the late 1960s, Josef Weigl's group in Germany and Shizuko Amagase's group in Japan each used chromatography to purify the proteolytic activity from several Nepenthes species, finding it to be most active at pH 2–3.[15][16][17] Amagase and Shigeru Nakayama proposed the name "Nepenthesin" for the responsible protease(s).[15] In 1998, Kenji Takahashi's group purified protein from 30 liters of Nepenthesia distillatoria fluid, finding activity similar to that previously described, and reporting part of the nepenthesin amino acid sequence.[15]
References
- ↑ "Enzymes from carnivorous plants (nepenthes). Isolation of the protease nepenthacin". FEBS Lett. 21 (3): 273–276. April 1972. doi:10.1016/0014-5793(72)80181-9. PMID 11946525.
- ↑ "The enzymes from carnivorous plants (Nepenthes): Properties and characterization of the acid protease nepenthacin". Planta Medica 55 (2): 227. 1989. doi:10.1055/s-2006-961979.
- ↑ 3.0 3.1 3.2 EC 3.4.23.12 - Nepenthesin. Integrated Enzyme Database (IntEnz).
- ↑ "Acid protease in Nepenthes. II. Study on the specificity of nepenthesin". J. Biochem. 66 (4): 431–9. October 1969. doi:10.1093/oxfordjournals.jbchem.a129166. PMID 5354017.
- ↑ "Digestive enzymes in insectivorous plants. 3. Acid proteases in the genus Nepenthes and Drosera peltata". J. Biochem. 72 (1): 73–81. July 1972. PMID 5069751.
- ↑ "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. September 1972. PMID 4634982.
- ↑ "Digestive enzymes secreted by the carnivorous plant Nepenthes macferlanei L". Planta 119 (1): 39–46. March 1974. doi:10.1007/BF00390820.
- ↑ James, Michael, ed (1998). "Acid Proteinase from Nepenthes distillatoria (Badura)". Aspartic proteinases: retroviral and cellular enzymes. New York: Plenum. pp. 453–458. ISBN 0-306-45809-8.
- ↑ "Variations in the content and isozymic composition of nepenthesin in the pitcher fluids among Nepenthes species". Carnivorous Plant Newsletter 36 (3): 73–76. 2007. http://www.carnivorousplants.org/cpn/articles/CPNv36n3p73_76.pdf.
- ↑ 10.0 10.1 "Stability Profiles of Nepenthesin in Urea and Guanidine Hydrochloride: Comparison with Porcine Pepsin A". Bioscience, Biotechnology, and Biochemistry 74 (11): 2323–2326. 2010. doi:10.1271/bbb.100391.
- ↑ "Acid Protease in Nepenthes: Partial Purification and Properties of the Enzyme". Proceedings of the Japan Academy 44 (5): 358–362. 1968. http://www.journalarchive.jst.go.jp/jnlpdf.php?cdjournal=pjab1945&cdvol=44&noissue=5&startpage=358&lang=en&from=jnlabstract.[yes|permanent dead link|dead link}}]
- ↑ "Enzymic and structural characterization of nepenthesin, a unique member of a novel subfamily of aspartic proteinases". Biochem. J. 381 (Pt 1): 295–306. July 2004. doi:10.1042/BJ20031575. PMID 15035659.
- ↑ "Expression and characterization of plant aspartic protease nepenthesin-1 from Nepenthes gracilis". Protein Expression and Purification 95: 121–128. March 2014. doi:10.1016/j.pep.2013.12.005.
- ↑ "The digestive fluid of Drosera indica contains a cysteine endopeptidase ("droserain") similar to dionain from Dionaea muscipula". Carnivorous Plant Newsletter 41 (4): 132–134. 2012.
- ↑ 15.0 15.1 15.2 15.3 "The enduring controversies concerning the process of protein digestion in Nepenthes (Nepenthaceae)". Carnivorous Plants Newsletter 29: 56–61. June 2000. https://cpn.carnivorousplants.org/articles/CPNv29n2p56_61.pdf. Retrieved 1 September 2021.
- ↑ "[Purification of the proteinase from Nepenthes pitcher secretion]" (in German). Planta 76 (3): 238–41. September 1967. doi:10.1007/BF00409815. PMID 24549466.
- ↑ "Acid protease in Nepenthes: Partial purification and properties of the enzyme". Proceedings of the Japan Academy 44 (5): 358–362. 1968. doi:10.2183/pjab1945.44.358.
External links
 |  |
