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

被引：37
作者：
Jo, Hye-Jin [1 ]
Park, Sunghoon [2 ]
Jeong, Hee-Gon [1 ]
Kim, Jung-Wan [3 ]
Park, Jong-Tae [1 ]
机构：
[1] Chungnam Natl Univ, Dept Food Sci & Technol, Taejon 305764, South Korea
[2] Res Inst Food & Biotechnol, SPC Grp, Seoul 151742, South Korea
[3] Incheon Natl Univ, Div Bioengn, Inchon 406771, South Korea
来源：
FEBS LETTERS | 2015年 / 589卷 / 10期
基金：
新加坡国家研究基金会;
关键词：
Glycogen branching enzymes (GBE); Branching pattern; N-terminal domain; Domain-manipulated mutant; Vibrio vulnificus; CARBOHYDRATE-BINDING MODULE; MALTOGENIC AMYLASE; SUBSTRATE-SPECIFICITY; BACTERIAL GLYCOGEN; PULLULANASE; METABOLISM; PATTERNS; FAMILY;
D O I：
10.1016/j.febslet.2015.03.011
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：1089 / 1094
页数：6
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