N-acetylglucosamine phosphotransferase

RCSB Protein Data Bank. NMR structure of the 140-315 fragment of the N-acetylglucosamine-1-phosphotransferase, alpha and beta subunits.</ref>.' scene='Alpha and Beta Subunits' />

References

1. ↑ Bioconjugate Chem., 2014, 25 (6), pp 1025–1030
2. ↑ Lodish, H. F., et al. Molecular cell biology, 8th ed.; W.H. Freeman-Macmillan Learning: New York, 2016.
3. ↑ Bao, M., Elmendorf, B. J., Booth, J. L., Drake, R. R., Canfield, W. M. Bovine UDP-N-acetylglucosamine:lysosomal-enzyme N-acetylglucosamine-1-phosphotransferase: II. Enzymatic characterization and identification of the catalytic subunit. J. Biol. Chem. 271: 31446-31451, 1996.<ref></ref>.

   Function

   Lysosomal enzymes are required for the detection of phosphotransferases in the Golgi apparatus. The structure of many of these lysosomal enzymes is unknown, so the interactions among such enzymes and N-acetylglucosamine phosphotransferase is largely undefined; one known fact is the lysine plays a major role.

   Yaghootfam et al. substituted lysine residues on the lysosomal arylsulfatases A and B to find any correlation between this substitution and phosphorylation. The results showed that the effects differed depending on the specific residue and its location on the arylsulfatases. Substitution of only lysine 457 on arylsulfatase A reduced phosphorylation by seventy-seven percent and increased release of the altered enzyme. The location of lysine 457 is in a helix, unlike typical lysine residues which are typically located in an unstructured loop. This could cause an effect, but lysines 497 and 507 were analyzed in arylsulfatases B with similar locations on the enzyme and there was no effect on the phosphorylation with the substitutions on arylsulfatases A and B. Yaghootfam et al. concluded that even homologous enzymes can vary in phosphorylation rates because of the great fluctuation in phosphotransferase recognition by lysosomal enzymes <ref>Journal of Biological Chemistry. 2003, Vol. 278 Issue 35, p32653-32661.</li>

   <li id="cite_note-3">[[#cite_ref-3|↑]] Hartz, P. A. N-Acetylglucosamine-1-phosphotransferase, Alpha/Beta Subunits; GNPTAB.</li> <li id="cite_note-4">[[#cite_ref-4|↑]] Canfield, W. M., Bao, M., Pan, J., Brewer, A. D. K., Pan, H., Roe, B., Raas-Rothschild, A. Mucolipidosis II and mucolipidosis IIIA are caused by mutations in the GlcNAc-phosphotransferase alpha/beta gene on chromosome 12p. Am. J. Hum. Genet. 63: A15 only, 1998.</li> <li id="cite_note-5">[[#cite_ref-5|↑]] Kudo, M., Bao, M., D'Souza, A., Ying, F., Pan, H., Roe, B. A., Canfield, W. M. The alpha- and beta-subunits of the human UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase are encoded by a single cDNA. J. Biol. Chem. 280: 36141-36149, 2005.</li> <li id="cite_note-6">[[#cite_ref-6|↑]] European Bioinformatics Institute. Protein Information Resource. SIB Swiss Institute of Bioinformatics.</li> <li id="cite_note-7">[[#cite_ref-7|↑]] Canfield, W. M., Bao, M., Pan, J., Brewer, A. D. K., Pan, H., Roe, B., Raas-Rothschild, A. Mucolipidosis II and mucolipidosis IIIA are caused by mutations in the GlcNAc-phosphotransferase alpha/beta gene on chromosome 12p. Am. J. Hum. Genet. 63: A15 only, 1998.</li> <li id="cite_note-8">[[#cite_ref-8|↑]] Hartz, P. A. N-Acetylglucosamine-1-phosphotransferase, Alpha/Beta Subunits; GNPTAB.</li>

   <li id="cite_note-9">[[#cite_ref-9|↑]] Kudo, M., Bao, M., D'Souza, A., Ying, F., Pan, H., Roe, B. A., Canfield, W. M. The alpha- and beta-subunits of the human UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase are encoded by a single cDNA. J. Biol. Chem. 280: 36141-36149, 2005.</li></ol></ref>

1. Bioconjugate Chem., 2014, 25 (6), pp 1025–1030. 2. Bao, M., Elmendorf, B. J., Booth, J. L., Drake, R. R., Canfield, W. M. Bovine UDP-N-acetylglucosamine:lysosomal-enzyme N-acetylglucosamine-1-phosphotransferase: II. Enzymatic characterization and identification of the catalytic subunit. J. Biol. Chem. 271: 31446-31451, 1996. 3. Journal of Biological Chemistry. 2003, Vol. 278 Issue 35, p32653-32661. 4. Canfield, W. M., Bao, M., Pan, J., Brewer, A. D. K., Pan, H., Roe, B., Raas-Rothschild, A. Mucolipidosis II and mucolipidosis IIIA are caused by mutations in the GlcNAc-phosphotransferase alpha/beta gene on chromosome 12p. Am. J. Hum. Genet. 63: A15 only, 1998. 5. Hartz, P. A. N-Acetylglucosamine-1-phosphotransferase, Alpha/Beta Subunits; GNPTAB. 6. Kudo, M., Bao, M., D'Souza, A., Ying, F., Pan, H., Roe, B. A., Canfield, W. M. The alpha- and beta-subunits of the human UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase are encoded by a single cDNA. J. Biol. Chem. 280: 36141-36149, 2005. 7. European Bioinformatics Institute. Protein Information Resource. SIB Swiss Institute of Bioinformatics. 8. Canfield, W. M., Bao, M., Pan, J., Brewer, A. D. K., Pan, H., Roe, B., Raas-Rothschild, A. Mucolipidosis II and mucolipidosis IIIA are caused by mutations in the GlcNAc-phosphotransferase alpha/beta gene on chromosome 12p. Am. J. Hum. Genet. 63: A15 only, 1998. 9. Lodish, H. F., et al. Molecular cell biology, 8th ed.; W.H. Freeman-Macmillan Learning: New York, 2016. 10. Q9UJJ9 N-acetylglucosamine-1-phosphotransferase subunit gamma. Swiss-Model. 2019. 11. RCSB Protein Data Bank. NMR structure of the 140-315 fragment of the N-acetylglucosamine-1-phosphotransferase, alpha and beta subunits.

Elizabeth Schneider Student; Erskine College, Due West, SC, United States