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Biochimie. 2008 May;90(5):830-4. doi: 10.1016/j.biochi.2008.01.013. Epub 2008 Feb 6.

Engineering and kinetic characterisation of two glucosyltransferases from Arabidopsis thaliana.

Author information

1
CNAP, Department of Biology (Area 8), University of York, York, YO10 5YW, UK.

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 Km towards the acceptor scopoletin. However, N1C3 had a Km 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.

PMID:
18295607
DOI:
10.1016/j.biochi.2008.01.013
[Indexed for MEDLINE]

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