UDP-N-acetylglucosamine transferase subunit ALG13 (ALG13)

UDP-N-acetylglucosamine transferase subunit ALG13 is an enzyme critically involved in the early steps of the N-linked glycosylation pathway in eukaryotes, functioning as the catalytic subunit of a heterodimeric complex with ALG14[1][2][3][5]. Within the endoplasmic reticulum, ALG13 catalyzes the addition of N-acetylglucosamine from UDP-GlcNAc to the growing dolichol-linked oligosaccharide precursor, representing the second step in the biosynthesis of the lipid-linked oligosaccharide essential for protein asparagine (N)-glycosylation[1][2][3][4][5][6]. Proper ALG13 function is indispensable for glycoprotein biosynthesis and thus for normal cellular and neurological development. Dysregulation or mutations in ALG13 cause congenital disorders of glycosylation and severe neurodevelopmental and epileptic syndromes, notably X-linked developmental and epileptic encephalopathy type 36 (DEE36)[1][3][5][6]. ALG13 is classified as a glycosyltransferase of the GT-B superfamily, with unique structural features that mediate activity in complex with ALG14[3][4].

Other names

Asparagine-linked glycosylation 13 homologUDP-N-acetylglucosaminyltransferase subunit ALG13CXorf45GLT28D1MDS031YGL047WFLJ23018TDRD13CDG1SGlycosyltransferase 28 domain-containing protein 1Tudor domain containing 13N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferaseDEE36EIEE36