The vertebrate sialylation machinery: structure-function and molecular evolution of GT-29 sialyltransferases.
Enzyme activity
Evolution
Sialic acid
Sialyltransferase
Structure-function
Journal
Glycoconjugate journal
ISSN: 1573-4986
Titre abrégé: Glycoconj J
Pays: United States
ID NLM: 8603310
Informations de publication
Date de publication:
08 2023
08 2023
Historique:
received:
05
01
2023
accepted:
10
05
2023
revised:
09
03
2023
medline:
13
7
2023
pubmed:
29
5
2023
entrez:
29
5
2023
Statut:
ppublish
Résumé
Every eukaryotic cell is covered with a thick layer of complex carbohydrates with essential roles in their social life. In Deuterostoma, sialic acids present at the outermost positions of glycans of glycoconjugates are known to be key players in cellular interactions including host-pathogen interactions. Their negative charge and hydrophilic properties enable their roles in various normal and pathological states and their expression is altered in many diseases including cancers. Sialylation of glycoproteins and glycolipids is orchestrated by the regulated expression of twenty sialyltransferases in human tissues with distinct enzymatic characteristics and preferences for substrates and linkages formed. However, still very little is known on the functional organization of sialyltransferases in the Golgi apparatus and how the sialylation machinery is finely regulated to provide the ad hoc sialome to the cell. This review summarizes current knowledge on sialyltransferases, their structure-function relationships, molecular evolution, and their implications in human biology.
Identifiants
pubmed: 37247156
doi: 10.1007/s10719-023-10123-w
pii: 10.1007/s10719-023-10123-w
pmc: PMC10225777
doi:
Substances chimiques
Sialyltransferases
EC 2.4.99.-
Sialic Acids
0
Glycoproteins
0
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
473-492Informations de copyright
© 2023. The Author(s).
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