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
Search PMC articles PubMed articles

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]

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: 227. doi:10.1055/s-2006-961979. 
3. ^ ^{a b c} 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. PMID 5354017. http://jb.oxfordjournals.org/cgi/content/abstract/66/4/431. 
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. http://jb.oxfordjournals.org/cgi/content/abstract/72/1/73. 
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 SBP, Inoue H, Iwamatsu A, Takahashi K (1998). "Acid Proteinase from Nepenthes distillatoria (Badura)". In James, Michael. 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". Carnivorous Plant News Letter 36 (3): 73–76. http://www.carnivorousplants.org/cpn/articles/CPNv36n3p73_76.pdf. 
10. ^ ^{a b} Kubota K, Metoki Y, Athauda SBP, 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. http://www.journalarchive.jst.go.jp/jnlpdf.php?cdjournal=pjab1945&cdvol=44&noissue=5&startpage=358&lang=en&from=jnlabstract. 
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1133788. 

External links

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