UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose = UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose. [EC:2.7.8.17]

UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity is a molecular function involved in the glycosylation of lysosomal enzymes. It catalyzes the transfer of N-acetylglucosamine-1-phosphate from UDP-N-acetylglucosamine to the asparagine residue of a lysosomal enzyme. This process is essential for the proper targeting of lysosomal enzymes to their destination within the lysosome. The enzyme responsible for this activity is known as N-acetylglucosamine-1-phosphotransferase (GlcNAc-1-phosphotransferase), a complex multimeric enzyme that consists of three subunits: alpha, beta, and gamma. The alpha subunit is responsible for binding UDP-N-acetylglucosamine and the gamma subunit binds the lysosomal enzyme. The beta subunit is thought to play a role in stabilizing the complex. The glycosylation of lysosomal enzymes by GlcNAc-1-phosphotransferase is a crucial step in the biosynthesis and maturation of these enzymes. It ensures their proper trafficking to the lysosome, where they are required for the degradation of macromolecules. Defects in this activity can lead to a variety of lysosomal storage disorders, characterized by the accumulation of undigested material in the lysosome.'
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Proteins (1)

Compounds (1)