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Waheed, A.; Hasilik, A.; von Figura, K.: UDP-N-acetylglucosamine:lysosomal enzyme precursor N-acetylglucosamine-1-phosphotransferase. Partial purification and characterization of the rat liver Golgi enzyme. J. Biol. Chem., 257, 12322–12331 (1982)
Zhao, K.W.; Yeh, R.; Miller, A.L.: Purification and characterization of human lymphoblast N-acetylglucosamine-1-phosphotransferase. Glycobiology, 2, 119–125 (1992)
Reitman, M.L.; Kornfeld, S.: Lysosomal enzyme targeting. N-Acetylglucosa-minylphosphotransferase selectively phosphorylates native lysosomal enzymes. J. Biol. Chem., 256, 11977–11980 (1981)
Waheed, A.; Pohlmann, R.; Hasilik, A.; von Figura, K.: Subcellular location of two enzymes involved in the synthesis of phosphorylated recognition markers in lysosomal enzymes. J. Biol. Chem., 256, 4150–4152 (1981)
Reitman, M.L.; Kornfeld, S.: UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase. Proposed enzyme for the phosphorylation of the high mannose oligosaccharide units of lysosomal enzymes. J. Biol. Chem., 256, 4275–4281 (1981)
Ben-Yoseph, Y.; Potier, M.; Pack, B.A.; Mitchell, D.A.; Melancon, S.B.; Nadler, H.L.: Molecular size of N-acetylglucosaminylphosphotransferase and α-N-acetylglucosaminyl phosphodiesterase as determined in situ in Golgi membranes by radiation inactivation. Biochem. J., 235, 883–886 (1986)
Hiller, A.M.; Koro, L.A.; Marchase, R.B.: Glucose-1-phosphotransferase and N-acetylglucosamine-1-phosphotransferase have distinct acceptor specificities. J. Biol. Chem., 262, 4377–4381 (1987)
Reitman, M.L.; Lang, L.; Kornfeld, S.: UDP-N-acetylglucosamine: lysosomal enzyme N-acetylglucosamine-1-phosphotransferase. Methods Enzymol., 107, 163–172 (1984)
Guillen, E.; Quesada-Allue, L.A.; Couso, R.O.: UDP-N-acetylglucosamine: glycoprotein N-acetylglucosamine-1-phosphotransferase activity in pupae of the Mediterranean fruit fly Ceratitis capitata. Insect Biochem. Mol. Biol., 24, 213–219 (1994)
Schierau, A.; Dietz, F.; Lange, H.; Schestag, F.; Parastar, A.; Gieselmann, V.: Interaction of arylsulfatase A with UDP-N-acetylglucosamine:lysosomal en-zyme-N-acetylglucosamine-1-phosphotransferase. J. Biol. Chem., 274, 3651–3658 (1999)
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)
Bao, M.; Booth, J.L.; Elmendorf, B.J.; Canfield, W.M.: Bovine UDP-N-acet-ylglucosamine:lysosomal-enzyme N-acetylglucosamine-1-phosphotransfer-ase. I. Purification and subunit structure. J. Biol. Chem., 271, 31437–31445 (1996)
Lukong, K.E.; Elsliger, M.A.; Mort, J.S.; Potier, M.; Pshezhetsky, A.V.: Identification of UDP-N-acetylglucosamine-phosphotransferase-binding sites on the lysosomal proteases, cathepsins A, B, and D. Biochemistry, 38, 73–80 (1999)
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(2008). UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase. In: Schomburg, D., Schomburg, I., Chang, A. (eds) Springer Handbook of Enzymes. Springer Handbook of Enzymes, vol 39. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-71524-5_17
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DOI: https://doi.org/10.1007/978-3-540-71524-5_17
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