Advanced search
Publication Cover
Bioscience, Biotechnology, and Biochemistry Volume 67, 2003 - Issue 9
Journal homepage
77
Views
0
CrossRef citations to date
0
Altmetric
Original Articles

Subsite Structure of Maltogenic Amylase from Thermomonospora viridis TF-35

Kosei TAKAHASHINihon Shokuhin Kako Co., Ltd.30 Tajima, Fuji-shi, Shizuoka 417-8530, Japan
&
Teruo NAKAKUKINihon Shokuhin Kako Co., Ltd.30 Tajima, Fuji-shi, Shizuoka 417-8530, Japan
Pages 1993-1995 | Received 10 Feb 2003, Accepted 16 May 2003, Published online: 22 May 2014

  • 1) Takahashi, K., Totsuka, A., Nakakuki, T., and Nakamura, N., Production and application of a maltogenic amylase by a strain of Thermomonospora viridis TF-35. Starch/stärke, 44, 96-101 (1992).
  • 2) Takahashi, K., Abe, J., Kozuma, T., Yoshida, M., Nakamura, N., and Hizukuri, S., Production and application of an isoamylase from Flavobacterium odoratum. Enzyme Microb. Technol., 19, 456-461 (1996).
  • 3) Suganuma, T., Matsuno, R., Onishi, M., and Hiromi, K., A study of the mechanism of action of TAKA-amylase A on linear oligosaccharides by product analysis and computer simulation. J. Biochem., 84, 293-316 (1978).
  • 4) Hidaka, H., On transglycosylation of α-amylase from Streptomyces sp. J. Jpn. Soc. Starch Sci., 30, 159-161 (1983).
  • 5) Suganuma, T., Mizukami, T., Moori, K., Onishi, M., and Hiromi, K., Studies of the action pattern of an α-amylase from Streptomyces praecox NA-273. J. Biochem., 88, 131-138 (1980).
  • 6) Outtrup, H., and Norman, B. E., Properties and application of a thermostable maltogenic amylase produced by a strain of Bacillus modified by recombinant-DNA techniques. Starch/stärke, 36, 405-411 (1984).
  • 7) Suganuma, T., Subsite structures and transglycosylation of Taka-amylase A and Bacillus subtilis saccharifying α-amylase. J. Jpn. Soc. Starch Sci., 30, 149-158 (1983).
  • 8) Nitta, Y., Mizushima, M., Hiromi, M., and Ono, S., Influence of molecular structures and analogues on Taka-amylase A catalyzed hydrolyses. J. Biochem., 69, 567-576 (1971).
  • . 1997. p. 6- 17.
  • 10) Muramatsu, Y., Takahashi, K., and Nakamura, N., Characterization of a maltogenic amylase of Thermomonospora viridis and application in branched cyclodextrin production. Starch/stärke, 45, 99-104 (1993).
  • 11) Matsui, I., Ishikawa, K., Matsui, E., Miyairi, S., Fukui, S., and Honda, K., Subsite structure of Saccharomycopsis α-amylase secreted from Saccharomyces cerevisiae. J. Biochem., 109, 566-569 (1991).
  • 12) Iwasa, S., Aoshima, H., Hiromi, K., and Hatano, H., Subsite affinities of bacterial liquefying α-amylase evaluated from the rate parameters of linear substrates. J. Biochem., 75, 969-978 (1974).
  • 13) Shimura, Y. Q., Wang, Q., and Sakano, Y., Subsite structure of α-amylase II from Thermoactinomyces vulgaris R-47. Biosci. Biotechnol. Biochem., 63, 2199-2201 (1999).
  • 14) Davis, G. J., Wilson, K. S., and Henrissat, B., Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem. J., 321, 557-559 (1997).

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:

Order Reprints Request Corporate Permissions

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:

Request Academic Permissions

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.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.