Journal
FEBS LETTERS
Volume 589, Issue 10, Pages 1089-1094Publisher
WILEY
DOI: 10.1016/j.febslet.2015.03.011
Keywords
Glycogen branching enzymes (GBE); Branching pattern; N-terminal domain; Domain-manipulated mutant; Vibrio vulnificus
Funding
- Basic Science Research Program through the National Research Foundation of Korea (NRF) - Ministry of Education, Science and Technology, Republic of Korea [2011-0014801]
- National Research Foundation of Korea [2011-0014801] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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The glycogen branching enzyme from Vibrio vulnificus (VvGBE) transfers short side chains (DP 3-5) significantly greater than any other bacterial glycogen branching enzyme (GBE). To elucidate the role of the N-domain of VvGBE in the unique branching pattern, domain-truncated (N1 and N) and N1-domain-swapped (with VvGBE N1 replacing the counter part of Escherichia coli GBE) mutants were constructed. The truncation mutants synthesized branched products with a greatly reduced proportion of short chains. The swapping mutant exhibited a branching pattern of the short chain region similar to that of VvGBE. We conclude that the N1-domain of VvGBE has a crucial role in the determination of the branching pattern of glycogen. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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