An active-site mutation causes enhanced reactivity and altered regiospecificity of transglucosylation catalyzed by the Bacillus sp. SAM 1606 α-glucosidase

Journal of Bioscience and Bioengineering

Volumn 89, Issue 5, 2000, Pages 431-437

  Inohara Ochiai, Misa ^a   Okada, Maki ^b   Nakayama, Toru ^c   Hemmi, Hisashi ^c   Ueda, Takashi ^b   Iwashita, Takashi ^d   Kan, Yukiko ^d   Shibano, Yuji ^b   Ashikari, Toshihiko ^b   Nishino, Tokuzo ^c  

^a SUNTORY LTD   (Japan)

^b KOBE GAKUIN UNIVERSITY   (Japan)

^c TOHOKU UNIVERSITY   (Japan)

^d SUNTORY INSTITUTE FOR BIOORGANIC RESEARCH   (Japan)

Author keywords

Bacillus; Regiospecificity; Transglucosylation; amylase family; glucosidase

Indexed keywords

AMINO ACIDS; BACTERIA; CATALYSIS; ENZYMES; SUBSTITUTION REACTIONS; SUGAR (SUCROSE);

BACILLUS SPECIES; GLUCOSIDASE; REGIOSPECIFICITY; TRANSGLUCOSYLATION;

ENZYME KINETICS;

AMINO ACID SUBSTITUTION; ARTICLE; BACILLUS; CATALYSIS; ENZYME ACTIVE SITE; ENZYME GLYCOSYLATION; NONHUMAN;

BACILLUS; BACILLUS CEREUS; BACILLUS SP.; NEGIBACTERIA; PROKARYOTA;

EID: 0033945034     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1389-1723(00)89092-1     Document Type: Article

References (26)

1. 1. Nakao, M., Nakayama, T., Harada, M., Kakudo, A., Ikemoto, H., Kobayashi, S., and Shibano, Y.: Purification and characterization of a thermostable α-glucosidase having transglucosylation activity of Bacillus sp. SAM1606. Appl. Microbiol. Biotech., 41, 337-343 (1994).
2. 2. Kelly, C. T. and Fogarty, W. M.: Microbial α-glucosidases. Process Biochem., 18, 6-12 (1983).
3. 3. Henrissat, B.: A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 280, 309-316 (1991).
4. 4. Henrissat, B. and Bairoch, A.: New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 293, 781-788 (1993).
5. 5. Svensson, B.: Regional distant sequence homology between amylases, α-glucosidase and transglucanosylases. FEBS Lett., 230, 72-76 (1988).
6. 6. Takata, H., Kuriki, T., Okada, S., Takesada, Y., Iizuka, M., Minamiura, N., and Imanaka, T.: Action of neopullulanase. Neopullulanase catalyzes both hydrolysis and transglycosylation at α-(1 → 4)-and α-(1 → 6)-glucosidic linkages. J. Biol. Chem., 267, 18447-18452 (1992).
7. 7. Svensson, B.: Protein engineering in the α-amylase family: catalytic mechanism, substrate specificity, and stability. Plant Mol. Biol., 25, 141-157 (1994).
8. 8. Kuriki, T. and Imanaka, T.: The concept of the α-amylase family: structural similarity and common catalytic mechanism. J. Biosci. Bioeng., 87, 557-565 (1999).
9. 9. Nakao, M., Nakayama, T., Kakudo, A., Inohara, M., Harada, M., Omura, F., and Shibano, Y.: Structure and expression of a gene coding for thermostable α-glucosidase with a broad substrate specificity from Bacillus sp. SAM 1606. Eur. J. Biochem., 220, 293-300 (1994).
10. 10. Watanabe, K., Kitamura, K., Iha, H., and Suzuki, Y.: Primary structure of the oligo-1,6-glucosidase of Bacillus cereus ATCC7064 deduced from the nucleotide sequence of the cloned gene. Eur. J. Biochem., 192, 609-620 (1990).
11. 11. Watanabe, K., Chishiro, K., Kitamura, K., and Suzuki, Y.: Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-1,6-glucosidase from Bacillus thermoglucosidasius KP1006. J. Biol. Chem., 266, 24287-24294 (1991).
12. 12. Matsuura, Y., Kusunoki, M., Harada, W., and Kakudo, M.: Structure and possible catalytic residues of Taka-amylase A. J. Biochem. (Tokyo), 95, 697-702 (1984).
13. 13. Qian, M., Haser, R., Buisson, G., Duee, E., and Payan, F.: The active center of a mammalian α-amylase. Structure of the complex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2.2-A resolution. Biochemistry, 33, 6284-6294 (1994) .
14. 14. Brayer, G. D., Luo, Y., and Withers, S. G.:The structure of human pancreatic α-amylase at 1.8 Ȧ resolution and comparisons with related enzymes. Protein Sci., 4, 1730-1742 (1995).
15. 15. Machius, M., Wiegand, G., and Huber, R.: Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 A resolution. J. Mol. Biol., 246, 545-559 (1995).
16. 16. Matsui, I., Yoneda, S., Ishikawa, K., Miyairi, S., Fukui, S., Umeyama, H., and Honda, K.: Roles of the aromatic residues conserved in the active center of Saccharomycopsis α-amylase for transglycosylation and hydrolysis activity. Biochemistry, 33, 451-458 (1994).
17. 17. Watanabe, K., Hata, Y., Kizaki, H., Katsube, Y., and Suzuki, Y.: The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 Ȧ resolution: structural characterization of proline-substitution sites for protein thermostabilization. J. Mol. Biol., 268, 142-153 (1997).
18. 18. Inohara-Ochiai, M., Nakayama, T., Goto, R., Nakao, M., Ueda, T., and Shibano, Y.: Altering substrate specificity of Bacillus sp. SAM1606 α-glucosidase by comparative site-specific mutagenesis. J. Biol. Chem., 272, 1601-1607 (1997).
19. 19. Shibano, Y., Yamagata, A., Nakamura, N., Iizuka, T., Sugisaki, H., and Takanami, M.: Nucleotide sequence coding for the insecticidal fragment of the Bacillus thuringiensis crystal protein. Gene (Amst.), 34, 243-251 (1985).
20. 20. Suzuki, Y. and Tanaka, R.: Production of p-nitrophenyl-α-D-glucopyranoside-hydrolyzing α-glucosidase by Bacillus cereus ATCC 7064. Eur. J. Appl. Microbiol. Biotechnol., 11, 161-165 (1981).
21. 21. Bradford, M. M.: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
22. 22. Suzuki, Y., Aoki, R., and Hayashi, H.: Assignment of p-nitrophenyl-α-D-glucopyranoside-hydrolyzing α-glucosidase of Bacillus cereus ATCC7064 to an exo-oligo-1,6-glucosidase. Biochim. Biophys. Acta, 704, 476-483 (1982).
23. 23. Penninga, D., Strokopytov, B., Roseboom, H. J., Lawson, C. L., Dijkstra, B. W., Bergsma, J., and Dijkhuizen, L.: Site-directed mutations in tyrosine 195 of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 affect activity and product specificity. Biochemistry, 34, 3368-3376 (1995).
24. 24. Kim, Y. H., Bae, K. H., Kim, T. J., Park, K. H., Lee, H. S., and Byun, S. M.: Effect on product specificity of cyclodextrin glycosyltransferase by site-directed mutagenesis. Biochem. Mol. Biol. Int., 41, 227-234 (1997).
25. 25. Fujiwara, S., Kakihara, H., Sakaguchi, K., and Imanaka, T.: Analysis of mutations in cyclodextrin glucanotransferase from Bacillus stearothermophilus which affect cyclization characteristics and thermostability. J. Bacteriol., 174, 7478-7481 (1992).
26. 26. Kuriki, T., Kaneko, H., Yanase, M., Takata, H., Shimada, J., Handa, S., Takada, T., Umeyama, H., and Okada, S.: Controlling substrate preference and transglycosylation activity of neopullulanase by manipulating steric constraint and hydrophobicity in active center. J. Biol. Chem., 271, 17321-17329 (1996).