Structural highlights
Function[GLGB_ORYSJ] Catalyzes the formation of the alpha-1,6-glucosidic linkages in starch by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position. Publication Abstract from PubMedStarch branching enzyme (SBE) catalyzes the cleavage of alpha-1,4-linkages and the subsequent transfer of alpha-1,4 glucan to form an alpha-1,6 branch point in amylopectin. We determined the crystal structure of the rice branching enzyme I (BEI) in complex with maltopentaose at a resolution of 2.2A. Maltopentaose bound to a hydrophobic pocket formed by the N-terminal helix, carbohydrate-binding module 48 (CBM48), and alpha-amylase domain. In addition, glucose moieties could be observed at molecular surfaces on the N-terminal helix (alpha2) and CBM48. Amino acid residues involved in the carbohydrate bindings are highly conserved in other SBEs, suggesting their generally conserved role in substrate binding for SBEs. Crystal structure of the rice branching enzyme I (BEI) in complex with maltopentaose.,Chaen K, Noguchi J, Omori T, Kakuta Y, Kimura M Biochem Biophys Res Commun. 2012 Aug 3;424(3):508-11. doi:, 10.1016/j.bbrc.2012.06.145. Epub 2012 Jul 3. PMID:22771800[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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