Identification of a bifunctional UDP-4-keto-pentose/UDP-xylose synthase in the plant pathogenic bacterium Ralstonia solanacearum strain GMI1000, a distinct member of the 4,6-dehydratase and decarboxylase family.

The Journal of Biological Chemistry
Xiaogang GuMaor Bar-Peled

Abstract

The UDP-sugar interconverting enzymes involved in UDP-GlcA metabolism are well described in eukaryotes but less is known in prokaryotes. Here we identify and characterize a gene (RsU4kpxs) from Ralstonia solanacearum str. GMI1000, which encodes a dual function enzyme not previously described. One activity is to decarboxylate UDP-glucuronic acid to UDP-beta-l-threo-pentopyranosyl-4''-ulose in the presence of NAD(+). The second activity converts UDP-beta-l-threo-pentopyranosyl-4''-ulose and NADH to UDP-xylose and NAD(+), albeit at a lower rate. Our data also suggest that following decarboxylation, there is stereospecific protonation at the C5 pro-R position. The identification of the R. solanacearum enzyme enables us to propose that the ancestral enzyme of UDP-xylose synthase and UDP-apiose/UDP-xylose synthase was diverged to two distinct enzymatic activities in early bacteria. This separation gave rise to the current UDP-xylose synthase in animal, fungus, and plant as well as to the plant Uaxs and bacterial ArnA and U4kpxs homologs.

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Jul 1, 2009·Journal of Biochemistry·Xiaogang GuMaor Bar-Peled

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Citations

Aug 10, 2011·Chemical Communications : Chem Comm·Sei-hyun ChoiHung-wen Liu
Aug 2, 2011·Journal of Bacteriology·Michael J CoyneLaurie E Comstock
Nov 30, 2011·PloS One·Yanbin YinYing Xu
Mar 5, 2011·Annual Review of Plant Biology·Maor Bar-Peled, Malcolm A O'Neill
Nov 5, 2015·Glycobiology·Wael ElhenawyMario F Feldman
Jun 3, 2015·Applied Microbiology and Biotechnology·Xu C DuanJosef Voglmeir
Jul 25, 2015·PloS One·Soyoun HwangMaor Bar-Peled
Aug 21, 2015·Chembiochem : a European Journal of Chemical Biology·Pauline Peltier-PainJon S Thorson
Mar 17, 2017·The Journal of Biological Chemistry·Zi LiMaor Bar-Peled

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