Related Experiment Video
Updated: May 6, 2026

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
Published on: November 25, 2017
CMP-Sialic Acid Synthetase: The Point of Constriction in the Sialylation Pathway
Melanie Sellmeier1, Birgit Weinhold, Anja Münster-Kühnel
1Institute for Cellular Chemistry, Hannover Medical School (MHH), Hannover, 30625, Germany.
Abstract:
Sialoglycoconjugates form the outermost layer of animal cells and play a crucial role in cellular communication processes. An essential step in the biosynthesis of sialylated glycoconjugates is the activation of sialic acid to the monophosphate diester CMP-sialic acid. Only the activated sugar is transported into the Golgi apparatus and serves as a substrate for the linkage-specific sialyltransferases. Interference with sugar activation abolishes sialylation and is embryonic lethal in mammals. In this chapter we focus on the enzyme catalyzing the activation of sialic acid, the CMP-sialic acid synthetase (CMAS), and compare the enzymatic properties of CMASs isolated from different species. Information concerning the reaction mechanism and active site architecture is included. Moreover, the unusual nuclear localization of vertebrate CMASs as well as the biotechnological application of bacterial CMAS enzymes is addressed.
Related Concept Videos
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Formation of Lipopolysaccharides
Protein Glycosylation
Glycosylation occurs in...
Phase II Reactions: Sulfation and Conjugation with α-Amino Acids
Biosynthesis of Polysaccharides
Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

