CEFOBI   05405
CENTRO DE ESTUDIOS FOTOSINTETICOS Y BIOQUIMICOS
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Kinetic and functional characterization of OTDSP, a phosphoglucan phosphatase from O. tauri.
Autor/es:
DIEGO FABIAN GOMEZ CASATI; MARTIN, M.; CARRILLO J.B.; BUSI, M. V.
Lugar:
Córdoba
Reunión:
Congreso; LII Reunión de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular (SAIB); 2016
Institución organizadora:
SAIB
Resumen:
Over the past decade, the phosphoglucan phosphataseshave surfaced as fundamental proteins that regulate storage carbohydratemetabolism in plants as well as mammals. The functional mechanism of theseenzymes is understood but little is known about its evolution in the greenlineage and no reports exits concerning green algae. In this sense, we haveidentified and characterized a novel glucan phosphatase of the ancient picoalgaOstreococcus tauri. We verified OtDSP phosphatase activity invitro with pNPP as well itsnatural substrate amylopectin, but with a different kinetic behavior. Tofurther characterize the enzyme and based in OtDSP homology with A. thaliana LSF2 we identified aminoacidic residues involved in catalysis and binding to substrate that weremutagenized. Wild type OtDSP and its mutants counterparts were studied by meansof native-PAGE, size exclusion chromatography and binding assays topolysaccharides. The results obtained suggest that OtDSP is a fully functionalenzyme in vivo.