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Probing the CMP‐Sialic Acid Donor Specificity of Two Human β‐ d ‐Galactoside Sialyltransferases (ST3Gal I and ST6Gal I) Selectively Acting on O‐ and N‐Glycosylproteins
Author(s) -
Noel Maxence,
Gilormini PierreAndré,
Cogez Virginie,
Yamakawa Nao,
Vicogne Dorothée,
Lion Cédric,
Biot Christophe,
Guérardel Yann,
HarduinLepers Anne
Publication year - 2017
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201700024
Subject(s) - sialic acid , chemistry , glycan , biochemistry , sialyltransferase , glycolipid , neuraminic acid , glycoprotein , n acetylneuraminic acid
Sialylation of glycoproteins and glycolipids is catalyzed by sialyltransferases in the Golgi of mammalian cells, whereby sialic acid residues are added at the nonreducing ends of oligosaccharides. Because sialylated glycans play critical roles in a number of human physio‐pathological processes, the past two decades have witnessed the development of modified sialic acid derivatives for a better understanding of sialic acid biology and for the development of new therapeutic targets. However, nothing is known about how individual mammalian sialyltransferases tolerate and behave towards these unnatural CMP‐sialic acid donors. In this study, we devised several approaches to investigate the donor specificity of the human β‐ d ‐galactoside sialyltransferases ST6Gal I and ST3Gal I by using two CMP‐sialic acids: CMP‐Neu5Ac, and CMP‐Neu5 N ‐(4pentynoyl)neuraminic acid (CMP‐Sia N Al), an unnatural CMP‐sialic acid donor with an extended and functionalized N‐acyl moiety.