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A common structural blueprint for plant UDP-sugar-producing pyrophosphorylases
Umeå University, Faculty of Science and Technology, Department of Plant Physiology.ORCID iD: 0000-0001-8685-9665
2011 (English)In: Biochemical Journal, ISSN 0264-6021, E-ISSN 1470-8728, Vol. 439, 375-379 p.Article, review/survey (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2011. Vol. 439, 375-379 p.
Keyword [en]
oligomerization, protein structure, sugar activation, UDP-sugar synthesis
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-50137DOI: 10.1042/BJ20110730ISI: 000296548300002OAI: oai:DiVA.org:umu-50137DiVA: diva2:460377
Available from: 2011-11-30 Created: 2011-11-28 Last updated: 2017-12-08Bibliographically approved

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Kleczkowski, Leszek A.

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