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A common structural blueprint for plant UDP-sugar-producing pyrophosphorylases
Leszek A Kleczkowski1, Matt Geisler, Elisabeth Fitzek
1Department of Plant Physiology, Umeå Plant Science Centre, Umeå University, Sweden. leszek.kleczkowski@plantphys.umu.se
Abstract:
Plant pyrophosphorylases that are capable of producing UDP-sugars, key precursors for glycosylation reactions, include UDP-glucose pyrophosphorylases (A- and B-type), UDP-sugar pyrophosphorylase and UDP-N-acetylglucosamine pyrophosphorylase. Although not sharing significant homology at the amino acid sequence level, the proteins share a common structural blueprint. Their structures are characterized by the presence of the Rossmann fold in the central (catalytic) domain linked to enzyme-specific N-terminal and C-terminal domains, which may play regulatory functions. Molecular mobility between these domains plays an important role in substrate binding and catalysis. Evolutionary relationships and the role of (de)oligomerization as a regulatory mechanism are discussed.
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