Sugar Activation for Production of Nucleotide Sugars as Substrates for Glycosyltransferases in Plants
2015 (English)In: Journal of Applied Glycoscience, ISSN 1880-7291, Vol. 62, no 2, 25-36 p.Article, review/survey (Refereed) Published
In order to serve as a glycosyl donor, a sugar or a sugar derivative (e.g. GlcA) needs to be “activated” to a highly energetic state of a nucleotide-sugar. This activation requires the involvement of specific enzymes which produce NDP-sugars (or, in one case, NMP-sugar), using NTP or NDP as substrate. The present review provides concise survey of distinct plant nucleotide-sugar pyrophosphorylases (all using NTP as one of the substrates and differing in sugar specificity) as well as nucleotide-sugar phosphorylases and sucrose synthase (all using NDP as one of substrates). The pyrophosphorylases discussed include UGPase, USPase, UAGPase, AGPase, GMPase (VTC1), and FKGP, whereas phosphorylases include ADP-Glc phosphorylase and GDP-Gal phosphorylase (VTC2/VTC5). We also discuss the activation mechanism of 3-deoxy-D-manno-octulosonic acid (Kdo) by CKS, leading to the formation of a unique NMP-linked sugar (CMP-Kdo).
Place, publisher, year, edition, pages
The Japanese Society of Applied Glycoscience , 2015. Vol. 62, no 2, 25-36 p.
Cell wall formation; glycosyltransferases; nucleotide sugars; sugar activation
Research subject Biochemistry
IdentifiersURN: urn:nbn:se:umu:diva-118718DOI: 10.5458/jag.jag.JAG-2015_003OAI: oai:DiVA.org:umu-118718DiVA: diva2:915687
FunderSwedish Research Council