HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Lang, L. Articles by Kornfeld, S. Search for Related Content PubMed PubMed Citation Articles by Lang, L. Articles by Kornfeld, S. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 261, Issue 14, 6320-6325, May, 1986

Glycoprotein phosphorylation in simple eucaryotic organisms. Identification of UDP-GlcNAc:glycoprotein N-acetylglucosamine-1- phosphotransferase activity and analysis of substrate specificity

L Lang, R Couso and S Kornfeld

UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1- phosphotransferase activity has been identified in both Acanthamoeba castellani and Dictyostelium discoideum. Each of these activities exhibits a different in vitro specificity toward various purified glycoproteins. The N-acetylglucosaminyl-phosphotransferase of A. castellani is very similar to the mammalian enzyme in that it phosphorylates the lysosomal enzymes cathepsin D and uteroferrin much more efficiently than nonlysosomal glycoproteins and appears to recognize a determinant on the protein portion of these good acceptors. In contrast the D. discoideum enzyme cannot utilize cathepsin D as a good substrate and, although it phosphorylates uteroferrin efficiently, it does not recognize the protein portion of this acceptor. The oligosaccharide of uteroferrin appears to assume a different conformation than the oligosaccharides of other glycoproteins and glycopeptides, as evidenced by its enhanced sensitivity to mannosidase digestion. This conformation, presumably induced by some interaction with the underlying protein, may be responsible for the specific phosphorylation of uteroferrin by the N- acetylglucosaminylphosphotransferase of D. discoideum.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				N. M Dahms, L. J Olson, and J.-J. P Kim Strategies for carbohydrate recognition by the mannose 6-phosphate receptors Glycobiology, September 1, 2008; 18(9): 664 - 678. [Abstract] [Full Text] [PDF]

				D. P. Mehta, J. R. Etchison, R. Wu, and H. H. Freeze UDP-GlcNAc:Ser-Protein N-Acetylglucosamine-1-Phosphotransferase from Dictyostelium discoideum Recognizes Serine-containing Peptides and Eukaryotic Cysteine Proteinases J. Biol. Chem., November 7, 1997; 272(45): 28638 - 28645. [Abstract] [Full Text] [PDF]

				M. Bao, J. L. Booth, B. J. Elmendorf, and W. M. Canfield Bovine UDP-N-acetylglucosamine:Lysosomal-enzyme N-Acetylglucosamine-1-phosphotransferase. I. PURIFICATION AND SUBUNIT STRUCTURE J. Biol. Chem., December 6, 1996; 271(49): 31437 - 31445. [Abstract] [Full Text] [PDF]

				M. Bao, B. J. Elmendorf, J. L. Booth, R. R. Drake, and W. M. Canfield Bovine UDP-N-acetylglucosamine:Lysosomal-enzyme N-Acetylglucosamine-1-phosphotransferase. II. ENZYMATIC CHARACTERIZATION AND IDENTIFICATION OF THE CATALYTIC SUBUNIT J. Biol. Chem., December 6, 1996; 271(49): 31446 - 31451. [Abstract] [Full Text] [PDF]

				S. Merello and R. Couso Characterization and Partial Purification of a Novel Enzymatic Activity J. Biol. Chem., March 31, 1995; 270(13): 7281 - 7287. [Abstract] [Full Text] [PDF]