文摘
We characterized a starch synthase III (SSIII) isoform from O. tauri which lacks starch binding domains (SBDs). Recombinant OsttaSSIII-C exhibited preference to branched glycans such as glycogen and amylopectin, rather than amylose. Results suggest a strong similarity between the active site of the O. tauri SSIII-C and other bacterial glycogen synthases. Mutations in residues R270, K275 and E352 affect OsttaSSIII-C catalytic activity.