Identification of catalytic amino acids of cyclodextran glucanotransferase from Bacillus circulans T-3040

Bioscience, Biotechnology and Biochemistry

Volumn 70, Issue 8, 2006, Pages 1947-1953

  Yamamoto, Tomoko ^a   Terasawa, Kazue ^a   Kim, Young Min ^b   Kimura, Atsuo ^b   Kitamura, Yoshiaki ^a   Kobayashi, Mikihiko ^c   Funane, Kazumi ^a  

^a NATIONAL FOOD RESEARCH INSTITUTE   (Japan)

^b HOKKAIDO UNIVERSITY   (Japan)

^c JISSEN WOMEN'S UNIVERSITY   (Japan)

Author keywords

Aspartate residue; Catalytic amino acid; Cyclodextran; Cyclodextran glucanotransferase

Indexed keywords

AMINO ACIDS; CARBOXYLATION; CATALYST ACTIVITY; ENZYMES; GLUCOSE; SUBSTRATES;

ASPARTATE RESIDUE; CATALYTIC AMINO ACID; CYCLODEXTRAN ENZYMES; CYCLODEXTRAN GLUCANOTRANSFERASE;

ENZYME KINETICS;

AMINO ACID; CYCLOISOMALTOOLIGOSACCHARIDE GLUCANOTRANSFERASE; GLUCOSYLTRANSFERASE; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS; BIOSYNTHESIS; CATALYSIS; CHEMISTRY; COMPARATIVE STUDY; ENZYME ACTIVE SITE; ENZYMOLOGY; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; GENETICS; ISOLATION AND PURIFICATION; MOLECULAR GENETICS; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; AMINO ACIDS; BACILLUS; CATALYSIS; CATALYTIC DOMAIN; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GLUCOSYLTRANSFERASES; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS;

BACILLUS CIRCULANS;

EID: 33747854147     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.60105     Document Type: Article

References (23)

1. Oguma, T., Tobe, K., and Kobayashi, M., Purification and properties of a novel enzyme from Bacillus spp. T-3040, which catalyzes the conversion of dextran to cyclic isomaltooligosaccharides. FEBS Lett., 345, 135-138 (1994).
2. Tilden, E. B., and Hudson, C. S., Conversion of starch to crystalline dextrins by the action of a new type of amylase separated from cultures of Aerobacillus macerans. J. Am. Chem. Soc., 63, 2900-2902 (1939).
3. Kobayashi, M., Funane, K., and Oguma, T., Inhibition of dextran and mutan synthesis by cycloisomaltooligosaccharides. Biosci. Biotechnol. Biochem., 59, 1861-1865 (1995).
4. Oguma, T., and Kawamoto, H., Production of cyclodextran and its application. Trends Glycosci. Glycotechnol., 15, 91-99 (2003).
5. Oguma, T., Kurokawa, T., Tobe, K., and Kobayashi, M., Cloning and sequence analysis of the cyclomaltooligosaccharide glucanotransferase gene from Bacillus circulans T-3040 and expression in Escherichia coli cells. J. Appl. Glycosci., 42, 415-419 (1995).
6. Henrissat, B., A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 280, 309-316 (1991).
7. Igarashi, T., Morisaki, H., Yamamoto, A., and Goto, N., An essential amino acid residue for catalytic activity of the dextranase of Streptococcus mutans. Oral Microbiol. Immunol., 17, 193-196 (2002).
8. van der Veen, B. A., Uitdehaag, J. C. M., Dijkstra, B. W., and Dijkhuizen, L., Engineering of cyclodextrin glycosyltransferase reaction and product specificity. Biochim. Biophys. Acta, 1543, 336-360 (2000).
9. Aoki, H., and Sakano, Y., A classification of dextran-hydrolysing enzymes based on amino-acid-sequence similarities. Biochem. J., 323, 859-861 (1997).
10. Funane, K., Nakai, S., Terasawa, K., Oguma, T., Kawamoto, H., Kitamura, Y., and Kobayashi, M., Mutation of Bacillus cyclodextran glycanotransferase to increase its reaction velocity. J. Appl. Glycosci., 50, 33-35 (2003).
11. Makrides, S. C., Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Rev., 60, 512-538 (1996).
12. Funane, K., Shiraiwa, M., Hashimoto, K., Ichishima, E., and Kobayashi, M., An active-site peptide containing the second essential carboxyl group of dextransucrase from Leuconostoc mesenteroides by chemical modifications. Biochemistry, 32, 13696-13702 (1993).
13. Xu, J., Bjursell, M. K., Himrod, J., Deng, S., Carmichael, L. K., Chiang, H. C., Hooper, L. V., and Gordon, J. I., A genomic view of the human-Bacterioides thetaiotaomicron symbiosis. Science, 299, 2074-2076 (2003).
14. Finnegan, P. M., Brumbley, S. M., O'Shea, M. G., Nevalainen, H., and Bergquist, P. L., Diverse dextranase genes from Paenibacillus species. Arch. Microbiol., 183, 140-147 (2005).
15. Igarashi, T., Yamamoto, A., and Goto, N., Sequence analysis of the Streptococcus mutans Ingbritt dexA gene encoding extracellular dextranase. Microbiol. Immunol., 39, 853-860 (1995).
16. Igarashi, T., Yamamoto, A., and Goto, N., Nucleotide sequence and molecular characterization of a dextranase gene from Streptococcus downei. Microbiol. Immunol., 45, 341-348 (2001).
17. Igarashi, T., Morisaki, H., and Goto, N., Molecular characterization of dextranase from Streptococcus rattus. Microbiol. Immunol., 48, 155-162 (2004).
18. Ohnishi, Y., Kubo, S., Ono, Y., Nozaki, M., Gonda, Y., Okano, H., Matsuya, T., Matsushiro, A., and Morita, T., Cloning and sequencing of the gene coding for dextranase from Streptococcus salivarius. Gene, 156, 93-96 (1995).
19. Wanda, S. Y., and Curtiss, R., 3rd., Purification and characterization of Streptococcus sobrinus dextranase produced in recombinant Escherichia coli and sequence analysis of the dextranase gene. J. Bacteriol., 176, 3839-3850 (1994).
20. Kawamoto, H., Oguma, T., Sekine, H., and Kobayashi, M., Immobilization of cycloisomaltooligosaccharide glucanotransferase for production of cycloisomaltooligosaccharides from dextran. Enzyme Microb. Technol., 28, 515-521 (2001).
21. 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).
22. Nakamura, A., Haga, K., Ogawa, S., Kuwano, K., Kimura, K., and Yamane, K., Functional relationships between cyclodextrin glucanotransferase from an alkalophilic Bacillus and α-amylases site-directed mutagenesis of the conserved two Asp and one Glu residues. FEBS Lett., 296, 37-40 (1992).
23. Strokopytov, B., Penninga, D., Rozeboom, H. J., Kalk, K. H., Dijkhuizen, L., and Dijkstra, B. W., X-ray structure of cyclodextrin glycosyltransferase complexed with acarbose: implications for the catalytic mechanism of glycosidases. Biochemistry, 34, 2234-2240 (1995).