Cyclization Reaction Catalyzed by Glycogen Debranching Enzyme (EC 2.4.1.25/EC 3.2.1.33) and Its Potential for Cycloamylose Production
Author:
Affiliation:
1. Biochemical Research Laboratory, Ezaki Glico Co., Ltd., Nishiyodogawa-ku, Osaka 555-8502, Japan
2. Institute of Cell and Molecular Biology, University of Edinburgh, Edinburgh EH9 3JH, United Kingdom
Abstract
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
Link
https://journals.asm.org/doi/pdf/10.1128/AEM.68.9.4233-4239.2002
Reference29 articles.
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2. Gessler, K., I. Uson, T. Takaha, N. Krauss, S. M. Smith, S. Okada, G. M. Sheldrick, and W. Saenger. 1999. V-amylose at atomic resolution: X-ray structure of a cycloamylose with 26 glucose residues (cyclomaltohexaicosaose). Proc. Natl. Acad. Sci. USA96:4246-4251.
3. Gillard, B. K., and T. E. Nelson. 1977. Amylo-1,6-glucosidase/4-α-glucanotransferase: use of reversible substrate model inhibitors to study the binding and active sites of rabbit muscle debranching enzyme. Biochemistry16:3978-3987.
4. Hizukuri, S., K. Shirasaka, and B. O. Juliano. 1983. Phosphorus and amylose branching in rice starch granules. Starch/Stärke35:348-350.
5. Imamura, H., S. Fushinobu, M. Yamamoto, T. Kumasaka, T. Wakagi, and H. Matsuzawa. 2001. Reaction mechanism and crystal structure of 4-α-glucanotransferase from a hyperthermophilic archaeon, Thermococcus litoralis. J. Appl. Glycosci.48:171-175.
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