Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase (ALG6)

Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase (ALG6) is an enzyme embedded in the endoplasmic reticulum membrane, belonging to the glycosyltransferase C-superfamily (GT-C). ALG6 initiates the final phase of lipid-linked oligosaccharide assembly for N-linked glycosylation by transferring the first glucose residue from dolichyl-phosphate-glucose to the Man9GlcNAc2-PP-dol intermediate, enabling subsequent steps in glycan maturation and optimal protein folding. Mutations in the ALG6 gene result in ALG6-CDG, a rare, autosomal recessive congenital disorder of glycosylation characterized by insufficient glycoprotein glycosylation and systemic symptoms, most notably neurological and gastrointestinal multitissue involvement. No drugs currently target ALG6 directly, and diagnosis relies on biochemical and genetic tests. The structure of ALG6 is characterized by transmembrane helices and essential catalytic aspartate residues crucial for function.

Other names

ALG6Alpha-1,3-glucosyltransferaseAsparagine-linked glycosylation protein 6 homologCDG1CDolichyl-P-Glc:Man(9)GlcNAc(2)-PP-dolichol alpha-1,3-glucosyltransferaseDolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferaseMan(9)GlcNAc(2)-PP-Dol alpha-1,3-glucosyltransferaseAsparagine-linked glycosylation 6 homolog (yeast, alpha-1,3-glucosyltransferase)My046

Not applicable as no drugs directly target ALG6. (Mechanism for hypothetical inhibitors: inhibition of glucosyltransferase activity in N-glycosylation pathway)