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豬籠草蛋白酶

維基百科，自由的百科全書
豬籠草蛋白酶
識別碼
EC編號 3.4.23.12
CAS號 9073-80-7
數據庫
IntEnz IntEnz瀏覽
BRENDA（英語：BRENDA） BRENDA入口
ExPASy（英語：ExPASy） NiceZyme瀏覽
KEGG KEGG入口
MetaCyc（英語：MetaCyc） 代謝路徑
PRIAM（英語：PRIAM_enzyme-specific_profiles） 概述
PDB RCSB PDB PDBj PDBe PDBsum

豬籠草蛋白酶（Nepenthesin，Nepenthacin[1][2]，Nepenthasin[3]），又稱豬籠草酸性蛋白酶，豬籠草天冬氨酸蛋白酶[3]是豬籠草捕蟲籠及盾葉茅膏菜（Drosera peltata）分泌的天冬氨酸蛋白酶。[4][5][6][7][8][9]其與胃蛋白酶類似，但其也能酶切兩側的天冬氨酸殘基及賴氨酸┼精氨酸。[3]其對pH值及溫度的穩定性高於豬胃蛋白酶A，對尿素及鹽酸胍的穩定性大大降低。[10]

1968年，Shigeru Nakayama和Shizuko Amagase以「nepenthesin」命名豬籠草蛋白酶。[11]在豬籠草屬中已確定了2個同工酶：豬籠草蛋白酶I與豬籠草蛋白酶II。[12]

參考文獻

[編輯]
  1. ^ Jentsch J. Enzymes from carnivorous plants (nepenthes). Isolation of the protease nepenthacin. FEBS Lett. April 1972, 21 (3): 273–276. PMID 11946525. doi:10.1016/0014-5793(72)80181-9. 
  2. ^ Jentsch J, Meierkord S, Hammer M. The enzymes from carnivorous plants (Nepenthes): Properties and characterization of the acid protease nepenthacin. Planta Medica. 1989, 55: 227. doi:10.1055/s-2006-961979. 
  3. ^ 3.0 3.1 3.2 EC 3.4.23.12 - Nepenthesin （頁面存檔備份，存於網際網路檔案館）. Integrated Enzyme Database (IntEnz).
  4. ^ Amagase S, Nakayama S, Tsugita A. Acid protease in Nepenthes. II. Study on the specificity of nepenthesin. J. Biochem. October 1969, 66 (4): 431–9. PMID 5354017. 
  5. ^ Amagase S. Digestive enzymes in insectivorous plants. 3. Acid proteases in the genus Nepenthes and Drosera peltata. J. Biochem. July 1972, 72 (1): 73–81. PMID 5069751. 
  6. ^ Amagase S, Mori M, Nakayama S. Digestive enzymes in insectivorous plants. IV. Enzymatic digestion of insects by Nepenthes secretion and Drosera peltata extract: proteolytic and chitinolytic activities. J. Biochem. September 1972, 72 (3): 765–7. PMID 4634982. 
  7. ^ Tökés ZA, Woon WC, Chambers SM. Digestive enzymes secreted by the carnivorous plant Nepenthes macferlanei L. Planta. March 1974, 119 (1): 39–46. doi:10.1007/BF00390820. 
  8. ^ Athauda SBP, Inoue H, Iwamatsu A, Takahashi K. Acid Proteinase from Nepenthes distillatoria (Badura). James, Michael (編). Aspartic proteinases: retroviral and cellular enzymes. New York: Plenum. 1998: 453–458. ISBN 0-306-45809-8. 
  9. ^ Takahashi K, Tanji M, Shibata C. Variations in the content and isozymic composition of nepenthesin in the pitcher fluids among Nepenthes species (PDF). Carnivorous Plant News Letter. 2007, 36 (3): 73–76 [2011-12-10]. （原始內容存檔 (PDF)於2012-02-27）. 
  10. ^ Kubota K, Metoki Y, Athauda SBP, Shibata C, Takahashi K. Stability Profiles of Nepenthesin in Urea and Guanidine Hydrochloride: Comparison with Porcine Pepsin A. Bioscience, Biotechnology, and Biochemistry. 2010, 74 (11): 2323–2326. doi:10.1271/bbb.100391. 
  11. ^ Nakayama S, Amagase S. Acid Protease in Nepenthes: Partial Purification and Properties of the Enzyme. Proceedings of the Japan Academy. 1968, 44 (5): 358–362. [永久失效連結]
  12. ^ Athauda SB, Matsumoto K, Rajapakshe S, Kuribayashi M, Kojima M, Kubomura-Yoshida N, Iwamatsu A, Shibata C, Inoue H, Takahashi K. Enzymic and structural characterization of nepenthesin, a unique member of a novel subfamily of aspartic proteinases. Biochem. J. July 2004, 381 (Pt 1): 295–306. PMC 1133788 可免費查閱. PMID 15035659. doi:10.1042/BJ20031575. 

擴展閱讀

[編輯]
  • The MEROPS online database for peptidases and their inhibitors: A01.040
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