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Engineering and kinetic characterisation of two glucosyltransferases from Arabidopsis thaliana
Research output: Contribution to journal › Article › peer-review
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Publication details
| Journal | BIOCHIMIE |
|---|---|
| Date | Published - May 2008 |
| Issue number | 5 |
| Volume | 90 |
| Number of pages | 5 |
| Pages (from-to) | 830-834 |
| Original language | English |
Abstract
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.
- protein engineering, glucosyltransferases, domain swapping, glycosylation, enzyme kinetics, ENZYME-CATALYZED REACTIONS, GLUTATHIONE-S-TRANSFERASE, CRYSTAL-STRUCTURE, BIOSYNTHETIC-PATHWAY, MEDICAGO-TRUNCATULA, MULTIGENE FAMILY, SMALL MOLECULES, GLYCOSYLTRANSFERASES, CLASSIFICATION, SIMILARITIES
Research areas
Projects
Exploiting genomics to make glycosidic bonds in vitro and metabolic engineering in vivo
Project: Research project (funded) › Research
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