By the same authors

From the same journal

Engineering and kinetic characterisation of two glucosyltransferases from Arabidopsis thaliana

Research output: Contribution to journalArticle

Published copy (DOI)

Author(s)

Department/unit(s)

Publication details

JournalBIOCHIMIE
DatePublished - May 2008
Issue number5
Volume90
Number of pages5
Pages (from-to)830-834
Original languageEnglish

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.

    Research areas

  • 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

Discover related content

Find related publications, people, projects, datasets and more using interactive charts.

View graph of relations