مطالعه بیوانفورماتیکی توالی‌های پروتئین آلیناز در گیاهان

مطالعه بیوانفورماتیکی توالی‌های پروتئین آلیناز در گیاهان

نوع مقاله : مقاله تحقیقاتی

چکیده

آلیناز (EC 4.4.1.4) آنزیمی وابسته به پیریدوکسال فسفات است که تبدیل آلین به آلیسین را انجام می‌دهد. آلیسین ترکیبی ارگانوسولفوره با ویژگی‌های ضد‌میکروبی، ضد‌سرطانی، ضد‌دیابتی و آنتی‌اکسیدانی است. مطالعه بر روی آلیناز و درک چگونگی تنظیم تولید آلیسین برای تولید در محل آن جهت مصارف کلنیکی ضروری است. در این مطالعه، توالی‌های پروتئین آلیناز گیاهی از سایت ExPASy و NCBI دریافت‌شدند و با ClustalW همردیفی صورت‌پذیرفت. نتایج این همردیفی شباهت 39-98 درصدی را میان توالی‌ها نشان‌داد. درخت فیلوژنی برای این توالی‌های پروتئینی با استفاده از نرم‌افزار MEGA4 و با روش نزدیکترین همسایه رسم‌شد. خانواده‌های Alliacea و Poaceae به خوبی در این درخت از هم تفکیک شده‌بودند. همچنین به کمک ابزارCD search موجود در سایت NCBI، EFG alliinase و AAT به عنوان دو دومین این پروتئین شناخته‌شدند.

کلیدواژه‌ها

عنوان مقاله [English]

Bioinformatics study of alliinase protein sequences in plants

چکیده [English]

Alliinase (EC 4.4.1.4) is a pyridoxal phosphate dependent enzyme which induces the conversion of alliin into allicin. Allicin is an organosulfur compound which has antimicrobial, anticancer, antidiabetic and antioxidant properties. A detailed study on the alliinase and regulation of allicin production are critical for on-site production of allicin for clinical usage. In this study, protein sequences of alliinase were obtained by ExPASy and NCBI and were aligned by using ClustalW. The sequence similarities range from approximately 39 -98%. A phylogenetic tree was built for the 10 alliinase protein sequences using MEGA4 by the Neighbor-Joining Method. Alliaceae and Poaceae families were separated carefully on the tree. Furthermore, EGF alliinase and AAT are two domain of allinase which were found by CD search of NCBI

کلیدواژه‌ها [English]

alliinase
allicin
Bioinformatics
phylogeny
Alignment

مراجع

1. Fry, F.H., Okarter, N., Baynton-Smith, C., Kershaw, M.J., Talbot, N.J., Jacob, C. 2005.Useof a substrate/alliinase combination to generate antifungal activity in situ. Journal of Agricultural and Food Chemistry. 53:574-580.

2. Hamamoto, A., Mazelis, M. 1986. The C-S lyases of higher-plants-isolation and properties of homogeneous cystinelyase from Broccoli (Brassica oleraceavar botrytis) buds. Plant Physiology. 80: 702-706.

3. Iwami, K.,Yasumoto, K. 1980. Alliinase-likeenzymes in fruiting bodies of Lentinus-edodes- their purification and substrate-specificity. Agricultural and Biological Chemistry.44: 3003-3004.

4. Jin, Y. N., Choi, Y.H., Yang, C.H. 2001. Identification of an essential tryptophan residue in alliinase from garlic (Allium sativum) by chemical modification. Bulletin of the Korean Chemical Society. 22(1):68-76.

5. Kamitani, H., Esaki, N., Tanaka, H., Imahara, H., Soda, K. 1990. Purification and characterization of S alkyl cysteine alpha, beta-lyase from Pseudomonasputida. Journal of Nutritional Science and Vitaminology. 36: 339-347.

6. Lancaster, J. E., Shaw, M. L., Joyce, M. D. P., McCallum, J. A., McManus, M. T. 2000. A novel alliinase from onion roots. Biochemical characterization and cDNA cloning. Plant Physiology. 122: 1269-1279.

7. Landshuter, J., Lohmuller, E. M.,Knobloch, K. 1994. Purification and characterization of C-S-lyase from Ramson, the wild garlic, Allium ursinum. Planta Medica. 60: 343-347.

8. Lohmuller, E. M., Landshuter, J.,Knobloch, K.1994. On the isolation and characterization of a C-Slyasepreparation from leek, Allium porrum.Planta Medica. 60: 337-342.

9. Londhe, V.P., Gavasane, A.T., Nipate, S.S., Bandawane, D.D., Chaudhari, P.D. 2011. Role of garlic (Allium sativum) in various diseases: An overview. Journal of Pharmaceutical Research and Opinion.1:(4) 129-134.

10. Manabe, T., Hasumi, A., Sugiyama, M., Yamazaki, M., Saito, K. 1998.Alliinase [S-alk(en)yl-L-cysteine sulfoxide lyase] from Allium tuberosum (Chinese chive). European Journal of Biochemistry. 257: 21-30.

11. Mazelis, M.,Creveling, R. K. 1975. Purification and properties of S-alkyl-L-cysteine lyase from seedlings of Acacia farnesiana Willd. Biochemical Journal. 147: 485-491.

12. Miron, T., Mironchik, M., Mirelman, D., Wilchek, M., Rabinkov, A. 2003. Inhibition of tumor growth by a novel approach: in situ allicin generation using targeted alliinase delivery. Molecular Cancer Therapeutics. 2:1295-1301.

13. Nock, L.P., Mazelis, M. 1987. The C-S lyases of higher plants: direct comparison of the physical properties of homogeneous alliinlyase of garlic (Allium sativum) and onion (Allium cepa). Plant Physiology. 85: 1079-1083.

14. Nomura, J., Nishizuka, Y.,Hayaishi, O. 1963. S Alkylcysteinase-enzymatic cleavage of S-methyl-Lcysteine and its sulfoxide. Journal of Biological Chemistry. 238: 1441-1446.

15. Rabinkov, A., Zhu, X. Z., Grafi, G., Galili, G.,Mirelman, D. 1994. Alliinlyase (alliinase) from garlic (Allium sativum). Biochemical characterization and cDNA cloning. Applied Biochemistry and Biotechnology.48: 149-171.

16. Scwimmer, S.,Mazelis, M. 1963. Characterization of alliinase of Allium cepa (onion). Archives of Biochemistry and Biophysics.100: 66-73.

17. Shadkchan, Y., Shemesh,E., Mirelman, D., Miron, T., Rabinkov, A., Wilchek, M., Osherov, N. 2004. Efficacy of allicin, the reactive molecule of garlic, in inhibiting Aspergillus spp. in vitro, and in a murine model of disseminated aspergillosis. Journal of Antimicrobial Chemotherapy, 53:832-836.

18. Shimon, L.J.W., Rabinkov, A., Shin, I., Miron, T.,Mirelman, D., Wilchek, M., Frolow, F. 2007.Two structures of alliinase from Alliium sativum L.: apoform and ternary complex with amino acrylatereaction intermediate covalently bound to the PLP cofactor. Journal of Molecular Biology. 366: 611-625.

19. VanDamme, E.J., Smeets, K., Torrekens, S., Van Leuven, F., Peumans, W.J. 1992. Isolationand characterization of alliinase cDNA clones from garlic (Allium sativumL.) and related species. European Journal of Biochemistry. 209:751-757.

20. Yutani, M., Taniguchi, H., Borjihan, H., Ogita, A., Fujita, K., Tanaka, T. 2011.Alliinase from Ensifer adhaerens and its use for generation of fungicidal activity. AMB Express. 1(2):1-8.