Actinidain
| actinidain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifiers | |||||||||
| EC number | 3.4.22.14 | ||||||||
| CAS number | 39279-27-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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Actinidain (EC 3.4.22.14, actinidin, Actinidia anionic protease, proteinase A2 of Actinidia chinensis) is a type of cysteine protease enzyme found in fruits including kiwifruit (genus Actinidia), pineapple, mango, banana and papaya. This enzyme is part of the papain-like peptidase C1 family.[1][2][3][4]
As a known allergen in kiwifruit,[5] the enzyme is under preliminary research for its effect on tight junction proteins of intestinal epithelial cells.[6][7]
Actinidain is commercially useful as a meat tenderizer[8][9] and in coagulating milk for dairy products.[10]
References
- ↑ Baker, E.N.; Boland, M.J.; Calder, P.C.; Hardman, M.J. (1980). "The specificity of actinidin and its relationship to the structure of the enzyme". Biochim. Biophys. Acta. 616 (1): 30–34. doi:10.1016/0005-2744(80)90260-0. PMID 7002215.
- ↑ Kamphuis, I.G.; Drenth, J.; Baker, E.N. (1985). "Thiol proteases. Comparative studies based on the high-resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H, and stem bromelain". J. Mol. Biol. 182 (2): 317–329. doi:10.1016/0022-2836(85)90348-1. PMID 3889350.
- ↑ Baker, E.N.; Drenth, J. (1987). "The thiol proteases: structure and mechanism". In Jurnak, F.A.; McPherson, A. Active Sites of Enzymes. Biological Macromolecules and Assemblies. 3. New York: John Wiley and Sons. pp. 314–368. ISBN 0-471-85142-6.
- ↑ Gul, S; Mellor, G. W.; Thomas, E. W.; Brocklehurst, K (2006). "Temperature-dependences of the kinetics of reactions of papain and actinidin with a series of reactivity probes differing in key molecular recognition features". Biochemical Journal. 396 (1): 17–21. doi:10.1042/BJ20051501. PMC 1449998
. PMID 16445383. - ↑ Maddumage, R; Nieuwenhuizen, N. J.; Bulley, S. M.; Cooney, J. M.; Green, S. A.; Atkinson, R. G. (2013). "Diversity and relative levels of actinidin, kiwellin, and thaumatin-like allergens in 15 varieties of kiwifruit (Actinidia)". Journal of Agricultural and Food Chemistry. 61 (3): 728–39. doi:10.1021/jf304289f. PMID 23289429.
- ↑ Grozdanovic, Milica M.; Čavić, Milena; Nešić, Andrijana; Andjelković, Uroš; Akbari, Peyman; Smit, Joost J.; Gavrović-Jankulović, Marija (2016-03-01). "Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions". Biochimica et Biophysica Acta (BBA) - General Subjects. 1860 (3): 516–526. doi:10.1016/j.bbagen.2015.12.005.
- ↑ Cavic, Milena; Grozdanovic, Milica M.; Bajic, Aleksandar; Jankovic, Radmila; Andjus, Pavle R.; Gavrovic-Jankulovic, Marija (2014-10-01). "The effect of kiwifruit (Actinidia deliciosa) cysteine protease actinidin on the occludin tight junction network in T84 intestinal epithelial cells". Food and Chemical Toxicology. 72: 61–68. doi:10.1016/j.fct.2014.07.012.
- ↑ Bekhit, A. A.; Hopkins, D. L.; Geesink, G; Bekhit, A. A.; Franks, P (2014). "Exogenous proteases for meat tenderization". Critical Reviews in Food Science and Nutrition. 54 (8): 1012–31. doi:10.1080/10408398.2011.623247. PMID 24499119.
- ↑ Eshamah, Hanan; Han, Inyee; Naas, Hesham; Acton, James; Dawson, Paul (2014-04-01). "Antibacterial effects of natural tenderizing enzymes on different strains of Escherichia coli O157:H7 and Listeria monocytogenes on beef". Meat Science. 96 (4): 1494–1500. doi:10.1016/j.meatsci.2013.12.010.
- ↑ Katsaros, George I.; Tavantzis, George; Taoukis, Petros S. (2010-01-01). "Production of novel dairy products using actinidin and high pressure as enzyme activity regulator". Innovative Food Science & Emerging Technologies. 11 (1): 47–51. doi:10.1016/j.ifset.2009.08.007.
External links
- The MEROPS online database for peptidases and their inhibitors: C01.007
- EC 3.4.22.14
- actinidain at the US National Library of Medicine Medical Subject Headings (MeSH)
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