Recent developments in studies on the characterization of properties a
nd functions of UDP-glucose pyrophosphorylase (UGPase) in plant metabo
lism are presented. UGPase constitutes a reversible enzymatic step for
interconversions between starch and sucrose metabolites, and is respo
nsible for synthesis and metabolism of UDP-glucose, a major form of nu
cleoside diphosphoglucose in plant cells. The enzyme, although conside
red not to have any regulatory function, has attracted considerable in
terest due to its ubiquitous distribution in plants, high activity, es
pecially in sink tissues, and because of the key role of UDP-glucose a
s a direct or indirect precursor of sucrose, starch and structural pol
ysaccharides. The enzyme has been the subject of biotechnological mani
pulations to engineer its kinetic properties and gene expression in re
lation to metabolic processes at the sucrose/starch interface. Dependi
ng on tissue type, the UGPase reaction may be channelled in vivo, eith
er toward UDP-glucose pyrophosphorolysis or synthesis, due to a metabo
lic coupling to other reactions of sugar pathways. Some strategies for
future research on plant UGPase are discussed.