Functional and structural differences between isoflavonoid β-glycosidases from Dalbergia sp.

Archives of Biochemistry and Biophysics

Volumn 468, Issue 2, 2007, Pages 205-216

  Chuankhayan, Phimonphan ^a   Rimlumduan, Thipwarin ^a   Tantanuch, Waraporn ^b   Mothong, Narumol ^a   Kongsaeree, Prachumporn T ^c   Metheenukul, Pornphimon ^a   Svasti, Jisnuson ^d   Jensen, Ole N ^e   Cairns, James R Ketudat ^a  

^a SURANAREE UNIVERSITY OF TECHNOLOGY   (Thailand)

^b National Synchrotron Research Center Thailand   (Thailand)

^c KASETSART UNIVERSITY   (Thailand)

^d MAHIDOL UNIVERSITY   (Thailand)

^e UNIVERSITY OF SOUTHERN DENMARK   (Denmark)

Author keywords

Glucosidase; 7 O d Apiofuranosyl (1 6) d glucopyranoside; Dalbergia cochinchinensis; Dalbergia nigrescens; Diglycosidase; Glycosyl hydrolase family 1; Glycosylation; Isoflavonoid glycoside; Plant; Substrate specificity

Indexed keywords

7 O BETA DEXTRO APIOSYL 1,6 BETA DEXTRO GLUCOSIDE DERIVATIVE; BETA GLYCOSIDASE; COMPLEMENTARY DNA; DALBERGIA EXTRACT; DALCOCHINASE; DALCOCHININ BETA DEXTRO GLUCOSIDE; DALNIGREIN; DALNIGREIN 7 O BETA DEXTRO APIOFURANOSYL 1,6 BETA DEXTRO GLUCOPYRANOSIDE; DALPATEIN; DALPATEIN 7 O BETA DEXTRO APIOFURANOSYL 1,6 BETA DEXTRO GLUCOPYRANOSIDE; GLUCOSIDE DERIVATIVE; GLYCOSIDASE; GLYCOSIDE; ISOFLAVONOID; PLANT EXTRACT; PROTEIN DNBGLU2; UNCLASSIFIED DRUG;

AMINO ACID ANALYSIS; ARTICLE; CHEMICAL BINDING; DALBERGIA; DALBERGIA COCHICHINENSIS; DALBERGIA NIGRESCENS; ENZYME STRUCTURE; GENE MUTATION; HYDROLYSIS; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PICHIA PASTORIS; PLANT SEED; PRIORITY JOURNAL; PROTEIN EXPRESSION; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; DALBERGIA; ENZYME ACTIVATION; GLYCOSIDE HYDROLASES; ISOFLAVONES; MOLECULAR SEQUENCE DATA; SEEDS; STRUCTURE-ACTIVITY RELATIONSHIP;

DALBERGIA; DALBERGIA COCHINCHINENSIS; DALBERGIA NIGRESCENS; PICHIA PASTORIS;

EID: 36148977206     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2007.09.015     Document Type: Article

References (33)

1. Henrissat B. Biochem. J. 280 (1991) 309-316
2. Mizutani M., Nakanishi H., Ema J.I., Ma S.J., Noguchi E., Inohara-Ochiai M., Fukuchi-Mizutani M., Nakao M., and Sakata K. Plant Physiol. 130 (2002) 2164-2176
3. Ogawa K., Ijima Y., Guo W., Watanabe N., Usui T., Dong S., Tong Q., and Sakata K. J. Agric. Food Chem. 45 (1997) 877-882
4. Suzuki H. Arch. Biochem. Biophys. 99 (1962) 476-483
5. Imaseki H., and Yamamoto T. Arch. Biochem. Biophys. 92 (1961) 467-474
6. Ahn Y.O., Mizutani M., Saino H., and Sakana K. J. Biol. Chem. 279 (2004) 23405-23414
7. Bourbouze R., Pratviel-Sosa F., and Percheron F. Phytochemistry 14 (1975) 1279-1282
8. Yasuda T., and Nakagawa H. Phytochemistry 37 (1994) 133-136
9. Kasai T., Kishimoto M., and Kawamura S. Kagawa Daigaku Nougakubu Gakujutsu Houkoku 32 (1981) 111-119
10. Hay G.W., Westlake D.W.S., and Simpson F.J. Can. J. Microbiol. 7 (1962) 921-93227
11. Hösel W., and Barz W. Eur. J. Biochem. 57 (1975) 607-616
12. Chuankhayan P., Hua Y., Svasti J., Sakdarat S., Sullivan P.A., and Ketudat-Cairns J.R. Phytochemistry 66 (2005) 1880-1889
13. Srisomsap C., Svasti J., Surarit R., Champattanachai V., Sawangareetrakul P., Boonpuan K., Subhasitanont P., and Chokchaichamnankit D. J. Biochem. 119 (1996) 585-590
14. Chuankhayan P., Rimlumduan T., Svasti J., and Ketudat-Cairns J.R. J. Agric. Food Chem. 55 6 (2007) 2407-2412
15. Svasti J., Srisomsap C., Techasakul S., and Surarit R. Phytochemistry 50 (1999) 739-743
16. Ketudat Cairns J.R., Champattanachai V., Srisomsap C., Wittman-Liebold B., Thiede B., and Svasti J. J. Biochem. 128 (2000) 999-1008
17. Frohman M. Methods Enzmol. 218 (1993) 340-356
18. Toonkool P., Metheenukul P., Sujiwattanarat P., Paiboon P., Tongtubtim N., Ketudat-Cairns M., Ketudat-Cairns J.R., and Svasti J. Protein Expr. Purif. 48 (2006) 195-204
19. Altschul S.F., Madden T.L., Schäffer A.A., Zhang J., Zhang Z., Miller W., and Lipman D.J. Nucleic Acids Res. 25 (1997) 3389-3402
20. Bendtsen J.D., Nielsen H., Heijne G., and Brunak S. J. Mol. Biol. 340 (2004) 783-795
21. Jeanmougin F., Thompson J.D., Gouy M., Higgins D.G., and Gibson T.J. Trends Biochem. Sci. 23 (1998) 403-405
22. Thompson J.D., Higgins D.G., and Gibson T.J. Nucleic Acids Res. 22 (1994) 4673-4680
23. J. Felsenstein, J: PHYLIP (Phylogeny Inference Package) version 3.6, Distributed by the author. Department of Genome Sciences, University of Washington, Seattle, 2005.
24. Guex N., and Peitsch M.C. Electrophoresis 18 (1997) 2714-2723
25. Charoenrat T., Ketudat-Cairns M., Stendahl-Andersen H., Jahic M., and Enfort S.O. Bioprocess Biosyst. Eng. 27 6 (2005) 399-406
26. Suzuki H., Takahashi S., Watanabe R., Fukushima Y., Fujita N., Noguchi A., Yokoyma R., Nishitani K., Nihino T., and Nakayama T. J. Biol. Chem. 281 (2006) 30251-30259
27. Barrett T., Suresh C.G., Tolley S.P., Dodson E.J., and Hughes M.A. Structure 3 (1995) 951-960
28. Czjzek M., Cicek M., Zamboni V., Bevan D.R., Henrissat B., and Esen A. Proc. Natl. Acad. Sci. USA 97 (2000) 13555-13560
29. Vyas N.K. Curr. Opin. Struct. Biol. 1 (1991) 732-740
30. Mildvan A.S., Weber D.J., and Kuliopulos A. Arch. Biochem. Biophys. 294 (1992) 327-340
31. Mildvan A.S. Biochemistry (USA) 43 (2004) 14517-14519
32. Verdoucq L., Czjzek M., Morinière J., Bevan D.R., and Esen A. J. Biol. Chem. 278 (2003) 25055-25062
33. Verdoucq L., Morinière J., Bevan D.R., Esen A., Vasella A., Henrissat B., and Czjzek M. J. Biol. Chem. 279 (2004) 31796-31803