EC Number   |
General Information |
Reference |
|---|
    2.7.7.43 | evolution |
enzyme AaCSS shares a common overall structure with Drosophila melanogaster CSS in terms of evolutionarily conserved motifs and the absence of the C-terminal domain typical to vertebrate CSSs |
761215 |
| 2.7.7.43 | evolution |
enzyme DmCSS shows a structure with evolutionarily conserved motifs and the absence of the C-terminal domain typical to vertebrate CSSs. The most prominent feature of Drosophila melanogaster CMP-Sia synthetase (DmCSS) is its Golgi-localization, contrasted with nuclear localization of vertebrate CSSs |
761215 |
| 2.7.7.43 | evolution |
enzyme TcCSS shares a common overall structure with Drosophila melanogaster CSS in terms of evolutionarily conserved motifs and the absence of the C-terminal domain typical to vertebrate CSSs |
761215 |
| 2.7.7.43 | malfunction |
cells lacking functional enzyme display increased viability during reovirus infection |
761773 |
| 2.7.7.43 | malfunction |
cleavage of the N-terminal hydrophobic region of the CSSs is critical for the enzyme activity |
761215 |
| 2.7.7.43 | malfunction |
mouse embryonic stem cell (mESC) lines that lack CMP-Sia synthetase (CMAS) and thereby the ability to activate Sia to CMP-Sia show that loss of CMAS activity results in an asialo cell surface accompanied by an increase in glycoconjugates with terminal galactosyl and oligo-LacNAc residues, as well as intracellular accumulation of free Sia. These changes do not impact intracellular metabolites or the morphology and transcriptome of pluripotent mESC lines. Moreover, the capacity of Cmas-/- mESCs for undirected differentiation into embryoid bodies, germ layer formation and even the generation of beating cardiomyocytes provides first and conclusive evidence that pluripotency and differentiation of mESC in vitro can proceed in the absence of (poly)sialoglycans. Genetic ablation of CMAS results in complete loss of cellsurface sialylation with concomitant increase in LacNAc structures. Intracellular Neu5Ac accumulation alters neither associated metabolites nor intracellular glycosylation |
760882 |
| 2.7.7.43 | metabolism |
the enzyme is involved in the biosynthesis of sialoglycoconjugates in vertebrates, overview |
760882 |
| 2.7.7.43 | physiological function |
CMAS activity is essential for maintaining cellular homeostasis of sialic acid biosynthesis |
760882 |
| 2.7.7.43 | physiological function |
CMP-sialic acid synthetase is a key enzyme in the biosynthesis of the capsular polysaccharides required for bacterial infection |
706038 |
| 2.7.7.43 | physiological function |
the enzyme gene is required for serotype 3 reovirus binding and infection of microglial cells |
761773 |
