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A more recent version of this article appeared on June 23, 2006
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M512727200v1
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Papers In Press, published online ahead of print April 27, 2006
J. Biol. Chem, 10.1074/jbc.M512727200
Submitted on November 29, 2005
Revised on April 27, 2006
Accepted on April 27, 2006

Distinct properties of the five UDP-D-glucose/UDP-D-galactose 4-epimerase isoforms of arabidopsis thaliana

Christine Barber, Johannes Rösti, Arun Rawat, Kim Findlay, Keith Roberts, and Georg J. Seifert

Cell and Developmental Biology, John Innes Institute, Norwich NR4 7UH

Corresponding Author: georg.seifert{at}bbsrc.ac.uk

Plant genomes contain genetically encoded isoforms of most nucleotide sugar interconversion enzymes. Here we show that A. thaliana has five genes encoding functional UDP-D-glucose/UDP-D-galactose 4-epimerase (named UGE1 to –5). All A. thaliana UDP-D-glucose 4-epimerase isoforms are dimeric in solution, maximally active in vitro at 30°C to 40°C and show good activity between pH 7 and pH 9. In vitro, UGE1, -3 and -5 act independently of externally added NAD+, while cofactor addition stimulates the activity of UGE2 and is particularly important for UGE4 activity. UGE1 and UGE3 are most efficiently inhibited by UDP. The five isoforms, display kcatUDP-Gal values between 23 and 128 sec-1 and KmUDP-Gal values between 0.1 and 0.3 mM. This results in enzymatic efficiencies ranging between 97 and 890 mM-1sec-1 for UGE4=UGE1


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