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

FEBS Letters

Potocki-Véronèse, Gabrielle¹  Gajhede, Michael²  Remaud-Simeon, Magali¹  Monsan, Pierre¹  Albenne, Cécile¹  Mirza, Osman²  Skov, Lars K² 

[1] Centre de Bioingénierie Gilbert Durand, UMR CNRS 5504, UMR INRA 792, INSA, 135 avenue de Rangueil, 31077 Toulouse Cedex 4, France;Protein Structure Group, Department of Chemistry, University of Copenhagen, Universitetsparken 5, DK-2100 Copenhagen, Denmark

关键词: Amylosucrase;    Sucrose;    Maltooligosaccharides;    Disproportionation;    Transglycosylation;    AS;    amylosucrase from Neisseria polysaccharea;    G2;    maltose;    G3;    maltotriose;    G4;    maltotetraose;    G5;    maltopentaose;    G6;    maltohexaose;    G7;    maltoheptaose;    pNP-G n;    paraNitroPhenyl-maltooligosaccharide with a degree of polymerisation of n;    TLC;    thin-layer chromatography;    HPLC;    high-performance liquid chromatography;   

DOI  :  10.1016/S0014-5793(02)03168-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 α-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.

【 授权许可】

Unknown