Nepenthesin

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Nepenthesin
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EC no. 3.4.23.12
CAS no. 9073-80-7
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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]

Contents

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]

Related Research Articles

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Nepenthes is a genus of carnivorous plants, also known as tropical pitcher plants, or monkey cups, in the monotypic family Nepenthaceae. The genus includes about 170 species, and numerous natural and many cultivated hybrids. They are mostly liana-forming plants of the Old World tropics, ranging from South China, Indonesia, Malaysia, and the Philippines; westward to Madagascar and the Seychelles (one); southward to Australia (four) and New Caledonia (one); and northward to India (one) and Sri Lanka (one). The greatest diversity occurs on Borneo, Sumatra, and the Philippines, with many endemic species. Many are plants of hot, humid, lowland areas, but the majority are tropical montane plants, receiving warm days but cool to cold, humid nights year round. A few are considered tropical alpine, with cool days and nights near freezing. The name "monkey cups" refers to the fact that monkeys were once thought to drink rainwater from the pitchers.

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<span class="mw-page-title-main">Plasmepsin</span> Group of Plasmodium enzymes

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<i>Nepenthes gracilis</i> Species of pitcher plant from Southeast Asia

Nepenthes gracilis, or the slender pitcher-plant, is a common lowland pitcher plant that is widespread in the Sunda region. It has been recorded from Borneo, Cambodia, Peninsular Malaysia, Singapore, Sulawesi, Sumatra, and Thailand. The species has a wide altitudinal distribution of 0 to 1100 m above sea level, although most populations are found below 100 m and plants are rare above 1000 m. Despite being a widespread plant, natural hybrids between N. gracilis and other species are quite rare.

<i>Nepenthes distillatoria</i> Species of pitcher plant from Sri Lanka

Nepenthes distillatoria is a tropical pitcher plant endemic to Sri Lanka. It was the second Nepenthes species to be described in print and the first to be formally named under the Linnaean system of taxonomy. It is therefore the type species of the genus.

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<span class="mw-page-title-main">Plant-specific insert</span>

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<span class="mw-page-title-main">Glutamic protease</span>

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References

  1. ↑ 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.
  2. ↑ 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.
  3. 1 2 3 EC 3.4.23.12 - Nepenthesin. Integrated Enzyme Database (IntEnz).
  4. ↑ 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. doi:10.1093/oxfordjournals.jbchem.a129166. PMID   5354017.
  5. ↑ 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.
  6. ↑ 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.
  7. ↑ 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.
  8. ↑ 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.
  9. ↑ 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.
  10. 1 2 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 .
  11. ↑ 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.[ permanent dead link ]
  12. ↑ 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.
  13. ↑ 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.
  14. ↑ 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.
  15. 1 2 3 4 Frazier CK (June 2000). "The enduring controversies concerning the process of protein digestion in Nepenthes (Nepenthaceae)" (PDF). Carnivorous Plants Newsletter. 29: 56–61. Retrieved 1 September 2021.
  16. ↑ Steckelberg R, Lüttge U, Weigl J (September 1967). "[Purification of the proteinase from Nepenthes pitcher secretion]". Planta (in German). 76 (3): 238–41. doi:10.1007/BF00409815. PMID   24549466.
  17. ↑ 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. doi: 10.2183/pjab1945.44.358 .
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