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Title: Transforming wheat vacuolar invertase into a high affinity sucrose:sucrose 1-fructosyltransferase
Authors: Schroeven, Lindsey ×
Lammens, Willem
Van Laere, André
Van den Ende, Wim #
Issue Date: Dec-2008
Publisher: Wiley-Blackwell Publishing Ltd.
Series Title: New Phytologist vol:180 issue:4 pages:822-831
Abstract: • Vacuolar invertases (VIs) degrade sucrose to glucose and fructose. Additionally,
the fructan plant wheat (Triticum aestivum) contains different fructosyltransferases
(FTs), which have evolved from VIs by developing the capacity to bind sucrose or
fructans as acceptor substrates. Modelling studies revealed a hydrogen bonding
network in the conserved WMNDPNG motif of VIs, which is absent in FTs.
• In this study, the hydrogen bonding network of wheat VI was disrupted by sitedirected
mutagenesis in the 23WMNDPNG29 motif. While the single mutants
(W23Y, N25S) showed a moderate increase in 1-kestose production, a synergistic
effect was observed for the double mutant (W23Y+N25S), showing a 17-fold
increase in transfructosylation capacity, and becoming a real sucrose:sucrose
1-fructosyltransferase.
• Vacuolar invertases are fully saturable enzymes, contrary to FTs. This is the first
report on the development of a fully saturable FT with respect to 1-kestose formation.
The superior kinetics (Km ~ 43 mM) make the enzyme useful for biotechnological
applications.
• The results indicate that changes in the WMNDPNG motif are necessary to
develop transfructosylating capability. The shift towards smaller and/or more
hydrophilic residues in this motif might contribute to the formation of a specific
acceptor site for binding of sugar, instead of water.
ISSN: 0028-646X
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Molecular Physiology of Plants and Micro-organisms Section - miscellaneous
Laboratory for Molecular Plant Physiology (-)
× corresponding author
# (joint) last author

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