Structural insight into L-ribulose 3-epimerase from Mesorhizobium loti

Acta Crystallographica Section D: Biological Crystallography

Volumn 69, Issue 12, 2013, Pages 2330-2339

  Uechi, Keiko ^a   Sakuraba, Haruhiko ^a   Yoshihara, Akihide ^a   Morimoto, Kenji ^a   Takata, Goro ^a  

^a KAGAWA UNIVERSITY   (Japan)

Author keywords

D psicose 3 epimerase; D tagatose 3 epimerase; L ribulose 3 epimerase; Thermostability

Indexed keywords

EPIMERASE; PENTOSE; RIBULOSE;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; D-PSICOSE 3-EPIMERASE; D-TAGATOSE 3-EPIMERASE; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYMOLOGY; L-RIBULOSE 3-EPIMERASE; MESORHIZOBIUM; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; TEMPERATURE; THERMOSTABILITY;

D-PSICOSE 3-EPIMERASE; D-TAGATOSE 3-EPIMERASE; L-RIBULOSE 3-EPIMERASE; THERMOSTABILITY;

AMINO ACID SEQUENCE; CARBOHYDRATE EPIMERASES; CATALYTIC DOMAIN; ENZYME STABILITY; MESORHIZOBIUM; MOLECULAR SEQUENCE DATA; PENTOSES; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY; TEMPERATURE;

EID: 84889854190     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444913021665     Document Type: Article

References (29)

1. Altschul, S. F., Gish, W., Miller, W., Myers, E. W. & Lipman, D. J. (1990). J. Mol. Biol. 215, 403-410.
2. Bradford, M. M. (1976). Anal. Biochem. 72, 248-254.
3. Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J.-S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T. & Warren, G. L. (1998). Acta Cryst. D54, 905-921.
4. Chan, H.-C., Zyu, Y., Hu, Y., Ko, T.-P., Huang, C.-H., Ren, F., Chen, C.-C., Ma, Y., Guo, R.-T. & Sun, Y. (2012). Protein Cell, 3, 123-131.
5. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. (2010). Acta Cryst. D66, 486-501.
6. Granström, T. B., Takata, G., Tokuda, M. & Izumori, K. (2004). J. Biosci. Bioeng. 97, 89-94.
7. Holm, L. & Rosenström, P. (2010). Nucleic Acids Res, 38, W545- W549.
8. Itoh, H., Okaya, H., Khan, A. R., Tajima, S., Hayakawa, S. & Izumori, K. (1994). Biosci. Biotechnol. Biochem. 58, 2168-2171.
9. Izumori, K. (2006). J. Biotechnol. 124, 717-722.
10. Kim, H.-J., Hyun, E.-K., Kim, Y.-S., Lee, Y.-J. & Oh, D.-K. (2006). Appl. Environ. Microbiol. 72, 981-985.
11. Kim, K., Kim, H.-J., Oh, D.-K., Cha, S.-S. & Rhee, S. (2006). J. Mol. Biol. 361, 920-931.
12. Laemmli, U. K. (1970). Nature (London), 227, 680-685.
13. Laurie, A. T. & Jackson, R. M. (2005). Bioinformatics, 21, 1908-1916.
14. Levin, G. V. (2002). J. Med. Food, 5, 23-36.
15. Lovell, S. C., Davis, I. W., Arendall, W. B., de Bakker, P. I., Word, J. M., Prisant, M. G., Richardson, J. S. & Richardson, D. C. (2003). Proteins, 50, 437-450.
16. Matsuo, T. & Izumori, K. (2004). Asia Pac. J. Clin. Nutr. 13, S127.
17. Matsuo, T., Tanaka, T., Hashiguchi, M., Izumori, K. & Suzuki, H. (2003). Asia Pac. J. Clin. Nutr. 12, 225-231.
18. Matthews, B. W. (1968). J. Mol. Biol. 33, 491-497.
19. McNicholas, S., Potterton, E., Wilson, K. S. & Noble, M. E. M. (2011). Acta Cryst. D67, 386-394.
20. Mu, W., Chu, F., Xing, Q., Yu, S., Zhou, L. & Jiang, B. (2011). Agric. Food Chem. 59, 7785-7792.
21. Murshudov, G. N., Skubák, P., Lebedev, A. A., Pannu, N. S., Steiner, R. A., Nicholls, R. A., Winn, M. D., Long, F. & Vagin, A. A. (2011). Acta Cryst. D67, 355-367.
22. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
23. Rodriguez, R., Chinea, G., Lopez, N., Pons, T. & Vriend, G. (1998). Bioinformatics, 14, 523-528.
24. Takeshita, K., Suga, A., Takada, G. & Izumori, K. (2000). J. Biosci. Bioeng. 90, 453-455.
25. Uechi, K., Takata, G., Fukai, Y., Yoshihara, A. & Morimoto, K. (2013). Biosci. Biotechnol. Biochem. 77, 511-515.
26. Vagin, A. & Teplyakov, A. (2010). Acta Cryst. D66, 22-25.
27. Winn, M. D. et al. (2011). Acta Cryst. D67, 235-242.
28. Yoshida, H., Yamada, M., Nishitani, T., Takada, G., Izumori, K. & Kamitori, S. (2007). J. Mol. Biol. 374, 443-453.
29. Zhang, L., Mu, W., Jiang, B. & Zhang, T. (2009). Biotechnol. Lett. 31, 857-862.