info:eu-repo/semantics/article
The unique nucleotide specificity of the sucrose synthase from Thermosynechococcus elongatus
Fecha
2013-01Registro en:
Figueroa, Carlos Maria; Asención Diez, Matías Damián; Kuhn, Misty L.; McEwen, Sheila; Salerno, Graciela Lidia; et al.; The unique nucleotide specificity of the sucrose synthase from Thermosynechococcus elongatus; Elsevier Science; FEBS Letters; 587; 2; 1-2013; 165-169
0014-5793
CONICET Digital
CONICET
Autor
Figueroa, Carlos Maria
Asención Diez, Matías Damián
Kuhn, Misty L.
McEwen, Sheila
Salerno, Graciela Lidia
Iglesias, Alberto Alvaro
Ballicora, Miguel A.
Resumen
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.