Literature DB >> 25819440

Vibrio vulnificus glycogen branching enzyme preferentially transfers very short chains: N1 domain determines the chain length transferred.

Hye-Jin Jo1, Sunghoon Park2, Hee-Gon Jeong1, Jung-Wan Kim3, Jong-Tae Park4.   

Abstract

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.
Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Branching pattern; Domain-manipulated mutant; Glycogen branching enzymes (GBE); N-terminal domain; Vibrio vulnificus

Mesh:

Substances:

Year:  2015        PMID: 25819440     DOI: 10.1016/j.febslet.2015.03.011

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


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