The unique nucleotide specificity of the sucrose synthase from Thermosynechococcus elongatus |
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Authors: | Carlos M Figueroa Matías D Asención Diez Misty L Kuhn Sheila McEwen Graciela L Salerno Alberto A Iglesias Miguel A Ballicora |
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Institution: | 1. Instituto de Agrobiotecnología del Litoral (UNL-CONICET), Facultad de Bioquímica y Ciencias Biológicas (UNL), Ciudad Universitaria, S3000ZAA Santa Fe, Argentina;2. Department of Chemistry and Biochemistry, Loyola University Chicago, 1032 W. Sheridan Rd., Chicago, IL 60660, USA;3. Centro de Estudios de Biodiversidad y Biotecnología (CEBB-MdP), INBA-CONICET, CIB, FIBA, Mar del Plata, Argentina |
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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. |
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