Maltooligosaccharide disproportionation reaction: an intrinsic property of amylosucrase from Neisseria polysaccharea

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Cécile Albenne, Lars K Skov, Osman Asghar Mirza, Michael Gajhede, Gabrielle Potocki-Véronèse, Pierre Monsan, Magali Remaud-Simeon

Amylosucrase from Neisseria polysaccharea (AS) is a remarkable transglycosidase of family 13 of the glycoside hydrolases that catalyses the synthesis of an amylose-like polymer from sucrose and is always described as a sucrose-specific enzyme. Here, we demonstrate for the first time the ability of pure AS to catalyse the disproportionation of maltooligosaccharides by cleaving the alpha-1,4 linkage at the non-reducing end of a maltooligosaccharide donor and transferring the glucosyl unit to the non-reducing end of another maltooligosaccharide acceptor. Surprisingly, maltose, maltotriose and maltotetraose are very poor glucosyl donors whereas longer maltooligosaccharides are even more efficient glucosyl donors than sucrose. At least five glucose units are required for efficient transglucosylation, suggesting the existence of strong binding subsites, far from the sucrose binding site, at position +4 and above.
OriginalsprogEngelsk
TidsskriftF E B S Letters
Vol/bind527
Udgave nummer1-3
Sider (fra-til)67-70
Antal sider4
ISSN0014-5793
DOI
StatusUdgivet - 11 sep. 2002

ID: 44864446