Engineering and kinetic characterisation of two glucosyltransferases from Arabidopsis thaliana

被引：38

作者：

Weis, Markus ^{[1
]}

Lim, Eng-Kiat ^{[1
]}

Bruce, Neil C. ^{[1
]}

Bowles, Dianna J. ^{[1
]}

机构：

[1] Univ York, Dept Biol, CNAP, Area 8, York YO10 5YW, N Yorkshire, England

来源：

BIOCHIMIE | 2008年 / 90卷 / 05期

关键词：

protein engineering; glucosyltransferases; domain swapping; glycosylation; enzyme kinetics;

D O I：

10.1016/j.biochi.2008.01.013

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：

This study describes the characterisation of a chimeric mutant derived from two arabidopsis glucosyltransferases, 71C1 and 71C3. A chimera, N1C3, was constructed to contain the N-terminal domain of 71C1 and the C-terminal domain of 71C3. The chimera and the wild-type GTs displayed a similar K-m towards the acceptor scopoletin. However, N1C3 had a K-m near identical to 71C3 towards UDP-glucose, but was three-fold lower than that of 71C1. The results suggest that the acceptor and sugar donor are recognised independently by the N- and C-terminal domain of the GTs respectively, and provide a foundation for the future design of glucosyltransferase biocatalysts through assembling domains with different affinity towards the acceptor and donor. (C) 2008 Elsevier Masson SAS. All rights reserved.

引用

页码：830 / 834

页数：5

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