UDPNacetylglucosamine1phosphotransferase

UDP-N-acetylglucosamine, commonly abbreviated UDP-GlcNAc, is an activated nucleotide sugar in which the N-acetylglucosamine moiety is linked to uridine diphosphate. It serves as an essential donor of N-acetylglucosamine in numerous glycosylation reactions across bacteria and eukaryotes and participates in the biosynthesis of key cellular polymers.

In bacteria, UDP-GlcNAc is a central precursor for cell wall biosynthesis. It is generated from fructose-6-phosphate through a pathway involving GlmS, GlmM, and GlmU, producing UDP-GlcNAc, which is subsequently used to form UDP-N-acetylmuramoyl-pentapeptide and other peptidoglycan building blocks. UDP-GlcNAc also contributes to the synthesis of lipopolysaccharide components in Gram-negative bacteria.

In eukaryotes, UDP-GlcNAc is produced mainly via the hexosamine biosynthetic pathway. Starting from fructose-6-phosphate, GFAT converts it to glucosamine-6-phosphate, followed by further processing to generate UDP-GlcNAc. This molecule provides GlcNAc for N-glycosylation and O-glycosylation reactions, including O-GlcNAcylation of cytosolic and nuclear proteins by O-GlcNAc transferase. It also serves as a donor for the synthesis of complex N-glycans in the endoplasmic reticulum and Golgi apparatus, as well as for other GlcNAc-dependent processes.

Overall, UDP-GlcNAc functions as a versatile activated sugar that links nutrient status to the regulation of glycosylation-dependent pathways in diverse organisms.