Identification of rice β-glucosidase with high hydrolytic activity towards salicylic acid β-d-glucoside

Bioscience, Biotechnology and Biochemistry

Volumn 77, Issue 5, 2013, Pages 934-939

  Himeno, Nami ^a   Saburi, Wataru ^a   Wakuta, Shinji ^a   Takeda, Ryosuke ^a   Matsuura, Hideyuki ^a   Nabeta, Kensuke ^a   Sansenya, Sompong ^b   Ketudat Cairns, James R ^b   Mori, Haruhide ^a   Imai, Ryozo ^c   Matsui, Hirokazu ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

^b SURANAREE UNIVERSITY OF TECHNOLOGY   (Thailand)

^c NATIONAL AGRICULTURAL RESEARCH CENTER FOR HOKKAIDO REGION   (Japan)

Author keywords

glucosidase; Rice; Salicylic acid; Substrate specificity; Tuberonic acid

Indexed keywords

AMMONIUM SULFATE PRECIPITATION; GLUCOSIDASE; HYDROLYTIC ACTIVITIES; PHYSIOLOGICAL SUBSTRATE; RECOMBINANT ENZYMES; RICE; RICE (ORYZA SATIVA L.); SUBSTRATE SPECIFICITY;

CARBOHYDRATES; ESCHERICHIA COLI; PHYSIOLOGICAL MODELS; SALICYLIC ACID; TUBES (COMPONENTS);

ENZYME ACTIVITY;

BETA GLUCOSIDASE; GLUCOSIDE; SALICYLIC ACID DERIVATIVE; SALICYLIC ACID GLUCOSIDE;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; HYDROLYSIS; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; PH; PICHIA; RICE; TEMPERATURE;

AMINO ACID SEQUENCE; BETA-GLUCOSIDASE; GLUCOSIDES; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; MOLECULAR SEQUENCE DATA; ORYZA SATIVA; PICHIA; SALICYLATES; SUBSTRATE SPECIFICITY; TEMPERATURE;

ESCHERICHIA COLI; ORYZA SATIVA; PICHIA PASTORIS; SOLANUM TUBEROSUM;

EID: 84878686598     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.120889     Document Type: Article

References (34)

1. Ketudat Cairns JR and Esen A, Cell. Mol. Life Sci., 67, 3389-3405 (2010).
2. Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B, Nucleic Acids Res., 37, D233-D238 (2009).
3. Schliemann W, J. Plant Physiol., 116, 123-132 (1984).
4. Brzobohatý B, Moore I, Kristoffersen P, Bako L, Campos N, Schell J, and Palme K, Science, 262, 1051-1054 (1993).
5. Lee KH, Piao HL, Kim HY, Choi SM, Jiang F, Hartung W, Hwang I, Kwak JM, and Lee IJ, Cell, 126, 1109-1120 (2006).
6. Xu ZY, Lee KH, Dong T, Jeong JC, Jin JB, Kanno Y, Kim DH, Kim SY, Seo M, Bressan RA, Yun DJ, and Hwang I, Plant Cell, 24, 2184-2199 (2012).
7. Wakuta S, Hamada S, Ito H, Matsuura H, Nabeta K, and Matsui H, Phytochemistry, 71, 1280-1288 (2010).
8. Wakuta S, Hamada S, Ito H, Imai R, Mori H, Matsuura H, Nabeta K, and Matsui H, J. Appl. Glycosci., 58, 67-70 (2010).
9. McConn M, Creelman RA, Bell E, Mullet JE, and Browse J, Proc. Natl. Acad. Sci. USA, 94, 5473-5477 (1997).
10. Vijayan P, Shockey J, Lévesque CA, Cook RJ, and Browse J, Proc. Natl. Acad. Sci. USA, 95, 7209-7214 (1998).
11. Staswick PE, Su W, and Howell SH, Proc. Natl. Acad. Sci. USA, 89, 6837-6840 (1992).
12. Fan X, Mattheis JP, and Fellman JK, Planta, 204, 444-449 (1998).
13. Stintzi A and Browse J, Proc. Natl. Acad. Sci. USA, 97, 10625-10630 (1992).
14. Opassiri R, Pomthong B, Onkoksoong T, Akiyama T, Esen A, and Ketudat Cairns JR, BMC Plant Biol., 6, 33 (2006).
15. Akiyama T, Kaku H, and Shibuya N, Phytochemistry, 48, 49-54 (1998).
16. Opassiri R, Maneesan J, Akiyama T, Pomthong B, Jin S, Kimura A, and Ketudat Cairns JR, Plant Sci., 179, 273-280 (2010).
17. Wang X, He R, and He G, J. Plant Physiol., 162, 1254-1262 (2005).
18. Vlot AC, Dempsey DA, and Klessig DF, Ann. Rev. Phytopathol., 47, 177-206 (2009).
19. Matsuura H, Ohmori F, Kobayashi M, Sakurai A, and Yoshihara T, Biosci. Biotechnol. Biochem., 64, 2380-2387 (2000).
20. Grynkiewicz G, Achmatowicz O, Hennig J, Indulski J, and Klessig DF, Pol. J. Chem., 67, 1251-1254 (1993).
21. Sansenya S, Ketudat Cairns JR, and Opassiri R, Acta Cystallogr. Sect. F Struct. Biol. Cryst. Commun., 66, 320-323 (2010).
22. Moore S and Stein WH, J. Biol. Chem., 176, 367-388 (1948).
23. Pluskal MG, Przekop MB, Kavonian MR, Vecoli C, and Hicks DA, Biotechniques, 4, 272-283 (1986).
24. Miwa I, Okudo J, Maeda K, and Okuda G, Clin. Chim. Acta, 37, 538-540 (1972).
25. Sansenya S, Opassiri R, Kuaprasert B, Chen C, and Ketudat Cairns JR, Arch. Biochem. Biophys., 510, 62-72 (2011).
26. Dempsey DA, Vlot AC, Wildermuth MC, and Klessig DF, The Arabidopsis Book, 9, e0156 (2011).
27. Lim E-K, Doucet CJ, Li Y, Elias L, Warrall D, Spencer SP, Ross J, and Bowles DJ, J. Biol. Chem., 277, 586-592 (2002).
28. Dean JV and Delaney SP, Physiol. Plant., 132, 417-425 (2008).
29. Song JT, Mol. Cells, 22, 233-238 (2006).
30. Umemura K, Satou J, Iwata M, Uozumi N, Koga J, Kawano T, Koshiba T, Anzai H, and Mitomi M, Plant J., 57, 463-472 (2009).
31. Hennig J, Malamy J, Grynkiewicz G, Indulski J, and Klessig DF, Plant J., 4, 593-600 (1993).
32. Hara-Nishimura I and Hatsugai N, Cell Death Differ., 18, 1298-1304 (2011).
33. Seto Y, Hamada S, Matsuura H, Matsushige M, Satou C, Takahashi K, Masuta C, Ito H, Matsui H, and Nabeta K, Pytochemistry, 70, 370-379 (2009).
34. Miersch O, Neumerkel J, Dippe M, Stenzel I, and Wasternack C, New Phytol., 177, 114-127 (2007).