α-(2,6)-sialyltransferase-catalyzed sialylations of conformationally constrained oligosaccharides

M. Carmen Galan; Andre P. Venot; John Glushka; Anne Imberty; Geert Jan Boons

doi:10.1021/ja0169771

α-(2,6)-sialyltransferase-catalyzed sialylations of conformationally constrained oligosaccharides

M. Carmen Galan, Andre P. Venot, John Glushka, Anne Imberty, Geert Jan Boons^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

It is demonstrated that conformationally restricted oligosaccharides can act as acceptors for glycosyltransferases. Correlation of the conformational properties of N-acetyl lactosamine (Galβ/(1-4)GlcNAc, LacNAc) and several preorganized derivatives with the corresponding apparent kinetic parameters of rat liver α-(2,6)-sialyltransferase-catalyzed sialylations revealed that this enzyme recognizes LacNAc in a low energy conformation. Furthermore, small variations in the conformational properties of the acceptors resulted in large differences in catalytic efficiency. Collectively, our data suggest that preorganization of acceptors in conformations that are favorable for recognition by a transferase may improve catalytic efficencies.

Original language	English
Pages (from-to)	5964-5973
Number of pages	10
Journal	Journal of the American Chemical Society
Volume	124
Issue number	21
DOIs	https://doi.org/10.1021/ja0169771
Publication status	Published - 20 May 2002
Externally published	Yes

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title = "α-(2,6)-sialyltransferase-catalyzed sialylations of conformationally constrained oligosaccharides",

abstract = "It is demonstrated that conformationally restricted oligosaccharides can act as acceptors for glycosyltransferases. Correlation of the conformational properties of N-acetyl lactosamine (Galβ/(1-4)GlcNAc, LacNAc) and several preorganized derivatives with the corresponding apparent kinetic parameters of rat liver α-(2,6)-sialyltransferase-catalyzed sialylations revealed that this enzyme recognizes LacNAc in a low energy conformation. Furthermore, small variations in the conformational properties of the acceptors resulted in large differences in catalytic efficiency. Collectively, our data suggest that preorganization of acceptors in conformations that are favorable for recognition by a transferase may improve catalytic efficencies.",

author = "Galan, {M. Carmen} and Venot, {Andre P.} and John Glushka and Anne Imberty and Boons, {Geert Jan}",

year = "2002",

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journal = "Journal of the American Chemical Society",

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T1 - α-(2,6)-sialyltransferase-catalyzed sialylations of conformationally constrained oligosaccharides

AU - Galan, M. Carmen

AU - Venot, Andre P.

AU - Glushka, John

AU - Imberty, Anne

AU - Boons, Geert Jan

PY - 2002/5/20

Y1 - 2002/5/20

N2 - It is demonstrated that conformationally restricted oligosaccharides can act as acceptors for glycosyltransferases. Correlation of the conformational properties of N-acetyl lactosamine (Galβ/(1-4)GlcNAc, LacNAc) and several preorganized derivatives with the corresponding apparent kinetic parameters of rat liver α-(2,6)-sialyltransferase-catalyzed sialylations revealed that this enzyme recognizes LacNAc in a low energy conformation. Furthermore, small variations in the conformational properties of the acceptors resulted in large differences in catalytic efficiency. Collectively, our data suggest that preorganization of acceptors in conformations that are favorable for recognition by a transferase may improve catalytic efficencies.

AB - It is demonstrated that conformationally restricted oligosaccharides can act as acceptors for glycosyltransferases. Correlation of the conformational properties of N-acetyl lactosamine (Galβ/(1-4)GlcNAc, LacNAc) and several preorganized derivatives with the corresponding apparent kinetic parameters of rat liver α-(2,6)-sialyltransferase-catalyzed sialylations revealed that this enzyme recognizes LacNAc in a low energy conformation. Furthermore, small variations in the conformational properties of the acceptors resulted in large differences in catalytic efficiency. Collectively, our data suggest that preorganization of acceptors in conformations that are favorable for recognition by a transferase may improve catalytic efficencies.

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AN - SCOPUS:0037140765

SN - 0002-7863

VL - 124

SP - 5964

EP - 5973

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 21

ER -

α-(2,6)-sialyltransferase-catalyzed sialylations of conformationally constrained oligosaccharides

Abstract

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