Document Detail


Characterization and partial purification of a novel enzymatic activity. UDP-GlcNAc:Ser-protein N-acetylglucosamine-1-phosphotransferase from the cellular slime mold Dictyostelium discoideum.
MedLine Citation:
PMID:  7706268     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
An enzymatic activity that transfers N-acetylglucosamine-1-phosphate residues from UDP-GlcNAc to serine units in proteins (UDP-GlcNAc:Ser-protein N-acetylglucosamine-1-phosphotransferase) was detected in membranes of the cellular slime mold Dictyostelium discoideum. The enzyme was partially purified by affinity chromatography in concanavalin A-Sepharose and ion exchange chromatography in a Mono Q column. The enzyme showed an absolute requirement for bivalent cations, Mn2+ being more effective than Mg2+. It had a broad optimum pH value (6.5-9.0). The Km for UDP-GlcNAc was 18 microM. In cell free assays it used apomucin and native or 8 M urea-denatured thyroglobulin but neither bovine serum albumin nor native or denatured uteroferrin as exogenous acceptors. Analysis of proteins isolated from cells grown in the presence of [32P]phosphate and from the culture medium showed that the majority of proteins bearing the structure Glc-NAc-1-P-Ser were secreted. In equilibrium density centrifugations of microsomes, the enzyme appeared in membranes having lighter densities than the enzyme that phosphorylates high mannose-type oligosaccharides. This showed that the activity that phosphorylates serine residues in proteins (UDP-GlcNAc:Ser-protein N-acetylglucosamine-1-phosphotransferase) is different from that phosphorylating protein-linked high mannose-type oligosaccharides (UDP-GlcNAc:glycoprotein N-acetylglucosamine-1-phosphotransferase).
Authors:
S Merello; A J Parodi; R Couso
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  270     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1995 Mar 
Date Detail:
Created Date:  1995-05-10     Completed Date:  1995-05-10     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  7281-7     Citation Subset:  IM    
Affiliation:
Instituto de Investigaciones Bioquímicas Fundación Campomar, Buenos Aires, Argentina.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Membrane / metabolism
Chromatography, Affinity
Chromatography, Ion Exchange
Dictyostelium / enzymology*
Glycosylation
Hydrogen-Ion Concentration
Kinetics
Magnesium / pharmacology
Manganese / pharmacology
Subcellular Fractions / enzymology
Substrate Specificity
Transferases (Other Substituted Phosphate Groups) / isolation & purification*,  metabolism*
Uridine Diphosphate N-Acetylglucosamine / metabolism
Chemical
Reg. No./Substance:
528-04-1/Uridine Diphosphate N-Acetylglucosamine; 7439-95-4/Magnesium; 7439-96-5/Manganese; EC 2.7.8.-/Transferases (Other Substituted Phosphate Groups); EC 2.7.8.-/UDP-GlcNAc - Ser-protein N-acetylglucosamine-1-phosphotransferase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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