186
Views
3
CrossRef citations to date
0
Altmetric
Original Articles

Molecular Cloning and Characterization of an Enzyme Hydrolyzing p-Nitrophenyl α-D-Glucoside from Bacillus stearothermophilus SA0301

, , , , , , & show all
Pages 495-499 | Received 20 Sep 2005, Accepted 30 Oct 2005, Published online: 22 May 2014

  • 1) Tonozuka, T., Sato, K., Sakaguchi, M., Suyama, K., Sekine, K., and Sakano, Y., Purification and some properties of an extracellular oligo-1,6-glucosidase from Bacillus stearothermophilus SA0301. J. Appl. Glycosci., 45, 397–400 (1998).
  • 2) Suzuki, Y., and Oishi, K., A relationship between efficiency of isomaltosaccharide hydrolysis and thermostability of six Bacillus oligo-1,6-glucosidases. Appl. Microbiol. Biotechnol., 31, 32–37 (1989).
  • 3) Watanabe, K., and Suzuki, Y., Protein thermostabilization by proline substitution. J. Mol. Cat. B: Enzymatic, 4, 167–180 (1998).
  • 4) Yamamoto, M., and Horikoshi, K., Purification and properties of an oligo-1,6-D-glucosidase from an alkalophilic Bacillus species. Carbohydr. Res., 197, 227–235 (1990).
  • 5) Chiba, S., Molecular mechanism in α-glucosidase and glucoamylase. Biosci. Biotechnol. Biochem., 61, 1233–1239 (1997).
  • 6) Nishio, T., Hakamata, W., Kimura, A., Chiba, S., Takatsuki, A., Kawachi, R., and Oku, T., Glycon specificity profiling of α-glucosidases using monodeoxy and mono-O-methyl derivatives of p-nitrophenyl α-D-glucopyranoside. Carbohydr. Res., 337, 629–634 (2002).
  • 7) 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).
  • 8) Noguchi, A., Yano, M., Ohshima, Y., Hemmi, H., Inohara-Ochiai, M., Okada, M., Min, K.-S., Nakayama, T., and Nishino, T., Deciphering the molecular basis of the broad substrate specificity of α-glucosidase from Bacillus sp. SAM1606. J. Biochem., 134, 543–550 (2003).
  • 9) Gotsche, S., and Dahl, M. K., Purification and characterization of the phospho-α(1,1)glucosidase (TreA) of Bacillus subtilis 168. J. Bacteriol., 177, 2721–2726 (1995).
  • 10) Rimmele, M., and Boos, W., Trehalose-6-phosphate hydrolase of Escherichia coli. J. Bacteriol., 176, 5654–5664 (1994).
  • 11) Russell, R. R. B., and Ferretti, J. J., Nucleotide sequence of the dextran glucosidase (dexB) gene of Streptococcus mutans. J. Gen. Microbiol., 136, 803–810 (1990).
  • 12) Janecek, Š., Svensson, B., and Henrissat, B., Domain evolution in the α-amylase family. J. Mol. Evol., 45, 322–331 (1997).
  • 13) Sambrook, J., Fritsch, E. F., and Maniatis, T., Molecular cloning: a laboratory manual, 2nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor (1989).
  • 14) Tonozuka, T., Mogi, S., Shimura, Y., Ibuka, A., Sakai, H., Matsuzawa, H., Sakano, Y., and Ohta, T., Comparison of primary structures and substrate specificities of two pullulan-hydrolyzing α-amylases, TVA I and TVA II, from Thermoactinomyces vulgaris R-47. Biochim. Biophys. Acta, 1252, 35–42 (1995).
  • 15) Page, R. D. M., TREEVIEW: an application to display phylogenetic trees on personal computers. Comput. Appl. Biosci., 12, 357–358 (1996).
  • 16) 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).
  • 17) MacGregor, E. A., Janecek, Š., and Svensson, B., Relationship of structure to specificity in the α-amylase family of enzymes. Biochim. Biophys. Acta, 1546, 1–20 (2001).
  • 18) Plumbridge, J., Regulation of gene expression in the PTS in Escherichia coli: the role and interactions of Mlc. Curr. Opin. Microbiol., 5, 187–193 (2002).
  • 19) Siebold, C., Flükiger, K., Beutler, R., and Erni, B., Carbohydrate transporters of the bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS). FEBS Lett., 504, 104–111 (2001).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.