Characterization of a novel carbohydrate binding domain of a putative amylase from Ostreococcus tauri

HEDIN, N.; BARCHIESI, J.; GOMEZ-CASATI, D.F.; BUSI, M.V.

MAR DEL PLATA

Congreso; 51 Annual Meeting Argentine Society for Biochemistry and Molecular Biology / LI Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular SAIB; 2015

SAIB

Starch Binding Domains (SBD) are one type ofcarbohydrate binding domains (CBM) that have acquired the evolutionaryadvantage of being able to interact and disrupt the substrate surface on aparticular way because they  present twopolysaccharide binding sites . The proteins containing this class of CBMs showa strong physical association with the different substrates, increasing therate of enzymatic reactions. These modules also occur in proteins with no hydrolyticactivity, constituting a core from which the catalytic proteins are organized.We are studying the starch metabolism of the picoeukaryote Ostreococcus tauri because even it has a small genome, this pathwaymaintain a complexity similar to Arabidopsisthaliana. In the present work, we characterized a predicted CBM20containing amylase of Ostreococcus tauri.We propose a possible molecular structure using bioinformatics modellingtechniques, and we analyze the binding properties of this module to differentinsoluble substrates. The results suggest that this particular CBM has a highaffinity for linear polysaccharides.