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- Title
The unique nucleotide specificity of the sucrose synthase from Thermosynechococcus elongatus
- Authors
Figueroa, Carlos M.; Asención Diez, Matías D.; Kuhn, Misty L.; McEwen, Sheila; Salerno, Graciela L.; Iglesias, Alberto A.; Ballicora, Miguel A.
- Abstract
Abstract: Sucrose synthase catalyzes the reversible conversion of sucrose and UDP into fructose and UDP-glucose. In filamentous cyanobacteria, the sucrose cleavage direction plays a key physiological function in carbon metabolism, nitrogen fixation, and stress tolerance. In unicellular strains, the function of sucrose synthase has not been elucidated. We report a detailed biochemical characterization of sucrose synthase from Thermosynechococcus elongatus after the gene was artificially synthesized for optimal expression in Escherichia coli. The homogeneous recombinant sucrose synthase was highly specific for ADP as substrate, constituting the first one with this unique characteristic, and strongly suggesting an interaction between sucrose and glycogen metabolism.
- Subjects
NUCLEOTIDES; SUCROSE synthase; THERMOSYNECHOCOCCUS elongatus; ESCHERICHIA coli; NITROGEN fixation; CARBON metabolism; URIDINE diphosphate sugars
- Publication
FEBS Letters, 2013, Vol 587, Issue 2, p165
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2012.11.011