Maltooligosaccharide disproportionation reaction: an intrinsic property of amylosucrase from Neisseria polysaccharea
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Maltooligosaccharide disproportionation reaction : an intrinsic property of amylosucrase from Neisseria polysaccharea. / Albenne, Cécile; Skov, Lars K; Mirza, Osman Asghar; Gajhede, Michael; Potocki-Véronèse, Gabrielle; Monsan, Pierre; Remaud-Simeon, Magali.
In: F E B S Letters, Vol. 527, No. 1-3, 11.09.2002, p. 67-70.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Maltooligosaccharide disproportionation reaction
T2 - an intrinsic property of amylosucrase from Neisseria polysaccharea
AU - Albenne, Cécile
AU - Skov, Lars K
AU - Mirza, Osman Asghar
AU - Gajhede, Michael
AU - Potocki-Véronèse, Gabrielle
AU - Monsan, Pierre
AU - Remaud-Simeon, Magali
PY - 2002/9/11
Y1 - 2002/9/11
N2 - 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.
AB - 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.
KW - Carbohydrate Conformation
KW - Glucosyltransferases
KW - Glycosylation
KW - Kinetics
KW - Maltose
KW - Neisseria
KW - Oligosaccharides
KW - Substrate Specificity
KW - Sucrose
KW - Trisaccharides
U2 - 10.1016/S0014-5793(02)03168-X
DO - 10.1016/S0014-5793(02)03168-X
M3 - Journal article
C2 - 12220635
VL - 527
SP - 67
EP - 70
JO - F E B S Letters
JF - F E B S Letters
SN - 0014-5793
IS - 1-3
ER -
ID: 44864446