Glycome Atlas
protein
Also known as glycosyltransferase, GT, sugar-transferring enzymes
Plain-language answer
Glycosyltransferases are the enzymes that build sugar chains. Each one takes an activated sugar and attaches it, in a specific place and orientation, to a growing glycan, protein, or lipid, so the cell assembles glycans in a controlled, stepwise way.1
Because these enzymes decide which sugars go where, their activity shapes blood group antigens, immune recognition, and how proteins fold and function. Inherited defects in them cause congenital disorders of glycosylation, and their activity changes in cancer.12
Technical detail
Glycosyltransferases catalyze transfer of a monosaccharide from an activated sugar nucleotide or lipid-linked donor to an acceptor, with defined donor, acceptor, and linkage specificity, and are classified into CAZy GT families.1
Most glycosyltransferases use nucleotide sugar donors (such as UDP-, GDP-, or CMP-sugars) and add the sugar to a specific hydroxyl of the acceptor with either retaining or inverting stereochemistry, giving each enzyme a defined product linkage.1
They act largely as an assembly line across the endoplasmic reticulum and Golgi, where their sequential, compartmentalized action produces the ordered glycan structures found on glycoproteins and glycolipids.12
Human relevance
Loss-of-function mutations in glycosyltransferases and related pathway genes cause congenital disorders of glycosylation with multisystem effects.1
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References