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5-azidouridine 5'-diphosphoglucose + glycoprotein D-mannose
?
-
-
-
-
?
UDP-glucose + glycoprotein D-mannose
UMP + glycoprotein 6-(D-glucose-1-phospho)-D-mannose
UDP-glucose + parafusin
?
UDP-glucose + phosphoglucomutase
?
additional information
?
-
UDP-glucose + glycoprotein D-mannose
UMP + glycoprotein 6-(D-glucose-1-phospho)-D-mannose
-
specific for UDP-glucose, endoglycosidase H-sensitive oligosaccharides on acceptor glycoproteins, primary acceptor in the chicken retina are peptides having apparent subunit MWs of 66000 and 62000
-
?
UDP-glucose + glycoprotein D-mannose
UMP + glycoprotein 6-(D-glucose-1-phospho)-D-mannose
-
specific for UDP-glucose, endoglycosidase H-sensitive oligosaccharides on acceptor glycoproteins, primary acceptor in the chicken retina are peptides having apparent subunit MWs of 66000 and 62000
-
?
UDP-glucose + glycoprotein D-mannose
UMP + glycoprotein 6-(D-glucose-1-phospho)-D-mannose
-
endogenous glycoprotein acceptor, the endogenous oligosaccharide acceptors for the GlcPTase are probably of high-mannose type, Glc-phosphotransferase may be involved in subcellular locallization of newly synthesized glycoproteins and its acceptors tagged by glucose 1-phosphate may comprise a particular group of glycoproteins destined for localization to the cell surface
-
?
UDP-glucose + glycoprotein D-mannose
UMP + glycoprotein 6-(D-glucose-1-phospho)-D-mannose
-
endogenous glycoprotein acceptor, the endogenous oligosaccharide acceptors for the GlcPTase are probably of high-mannose type, Glc-phosphotransferase may be involved in subcellular locallization of newly synthesized glycoproteins and its acceptors tagged by glucose 1-phosphate may comprise a particular group of glycoproteins destined for localization to the cell surface
-
?
UDP-glucose + glycoprotein D-mannose
UMP + glycoprotein 6-(D-glucose-1-phospho)-D-mannose
-
specific for UDP-glucose, endoglycosidase H-sensitive oligosaccharides on acceptor glycoproteins, primary acceptor in the chicken retina are peptides having apparent subunit MWs of 66000 and 62000
-
?
UDP-glucose + glycoprotein D-mannose
UMP + glycoprotein 6-(D-glucose-1-phospho)-D-mannose
-
the 35S-labeled phosphorothioate analogue of UDP-glucose is used by this enzyme with high efficiency
-
?
UDP-glucose + glycoprotein D-mannose
UMP + glycoprotein 6-(D-glucose-1-phospho)-D-mannose
-
-
-
?
UDP-glucose + glycoprotein D-mannose
UMP + glycoprotein 6-(D-glucose-1-phospho)-D-mannose
-
acceptor protein is cytoplasmic and is glycosylated by the enzyme at a site accessible to cytoplasm, the acceptor of 62 kDa is not phosphoglucomutase but the active site serine of this enzyme can be phosphorylated by radio labeled sugar phosphate present as a trace contaminant
-
?
UDP-glucose + glycoprotein D-mannose
UMP + glycoprotein 6-(D-glucose-1-phospho)-D-mannose
-
acceptor protein is cytoplasmic and is glycosylated by the enzyme at a site accessible to cytoplasm, the acceptor of 62 kDa is not phosphoglucomutase but the active site serine of this enzyme can be phosphorylated by radio labeled sugar phosphate present as a trace contaminant
-
?
UDP-glucose + glycoprotein D-mannose
UMP + glycoprotein 6-(D-glucose-1-phospho)-D-mannose
-
the 35S-labeled phosphorothioate analogue of UDP-glucose is used by this enzyme with high efficiency
-
?
UDP-glucose + glycoprotein D-mannose
UMP + glycoprotein 6-(D-glucose-1-phospho)-D-mannose
-
the 35S-labeled phosphorothioate analogue of UDP-glucose is used by this enzyme with high efficiency
-
?
UDP-glucose + glycoprotein D-mannose
UMP + glycoprotein 6-(D-glucose-1-phospho)-D-mannose
-
-
-
?
UDP-glucose + glycoprotein D-mannose
UMP + glycoprotein 6-(D-glucose-1-phospho)-D-mannose
-
-
-
?
UDP-glucose + parafusin
?
-
parafusin is the principal acceptor for GlcPTase in Paramecium tetraurelia and it is evidently associated with membrane fusion during exocytosis, its cytoplasmic glycosylation by GlcPTase has a regulatory role
-
-
?
UDP-glucose + parafusin
?
-
reversible phosphoglycosylation of parafusin could play an important role in signal transduction during secretion in Paramecium tetraurelia, a protein evidently associated with membrane fusion during exocytosis
-
-
?
UDP-glucose + phosphoglucomutase
?
-
-
-
-
?
UDP-glucose + phosphoglucomutase
?
-
specific for UDP-glucose, the site affected in the GlcPTase reaction is not the enzymatic active site of phosphoglucomutase, underglucosylated forms of phosphoglucomutase obtained in response to heat shock and growth in media containing carbon sources other than glucose increase transfer in vitro GlcPTase assays and appear to reflect regulation of the GlcPTase activity
-
-
?
UDP-glucose + phosphoglucomutase
?
-
underglucosylated phosphoglucomutase increases GlcPTase activity in vitro, this underglucosylated state is maximized when galactose is used as carbon source or following a heat shock in Saccharomyces cerevisiae cultures
-
-
?
additional information
?
-
-
may be a controlling enzyme for targeting of certain newly synthesized proteins to the cell surface
-
-
?
additional information
?
-
-
GlcPTase from Saccharomyces cerevisiae recognizes and reacts with GlcPTase acceptor from Rattus norvegicus. The reciprocal experiment also results in glucose phosphate transfer demonstrating that this glycosylation reaction has been conserved during the evolution. Phosphoglucomutase from rabbit muscle can also act as an acceptor
-
-
?
additional information
?
-
-
GlcPTase from Saccharomyces cerevisiae recognizes and reacts with GlcPTase acceptor from Rattus norvegicus. The reciprocal experiment also results in glucose phosphate transfer demonstrating that this glycosylation reaction has been conserved during the evolution. Phosphoglucomutase from rabbit muscle can also act as an acceptor
-
-
?
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Koro, L.A.; Marchase, R.B.
A UDP-glucose:glycoprotein glucose-1-phosphotransferase in embryonic chicken neural retina
Cell
31
739-748
1982
Gallus gallus
brenda
Satir, B.H.; Srisomsap, C.; Reichman, M.; Marchase, R.B.
Parafusin, an exocytic-sensitive phosphoprotein, is the primary acceptor for the glucosylphosphotransferase in Paramecium tetraurelia and rat liver
J. Cell Biol.
111
901-907
1990
Paramecium tetraurelia, Rattus norvegicus
brenda
Srisomsap, C.; Richardson, K.L.; Jay, J.C.; Marchase, R.B.
Localization of the glucose phosphotransferase to a cytoplasmically accessible site on intracellular membranes
J. Biol. Chem.
263
17792-17797
1988
Rattus norvegicus
brenda
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
Gallus gallus, Homo sapiens
brenda
Marchase, R.B.; Richardson, K.L.; Srisomsap, C.; Drake, R.R.; Haley, B.E.
Resolution of phosphoglucomutase and the 62-kDa acceptor for the glucosylphosphotransferase
Arch. Biochem. Biophys.
280
122-129
1990
Rattus norvegicus
brenda
Marchase, R.B.; Bounelis, P.; Brumley, L.M.; Dey, N.; Browne, B.; Auger, D.; Fritz, T.A.; Kulesza, P.; Bedwell, D.M.
Phosphoglucomutase in Saccharomyces cerevisiae is a cytoplasmic glycoprotein and the acceptor for a Glc-phosphotransferase
J. Biol. Chem.
268
8341-8349
1993
Saccharomyces cerevisiae, Rattus norvegicus
brenda
Dey, N.B.; Bounelis, P.; Fritz, T.A.; Bedwell, D.M.; Marchase, R.B.
The glycosylation of phosphoglucomutase is modulated by carbon source and heat shock in Saccharomyces cerevisiae
J. Biol. Chem.
269
27143-27148
1994
Saccharomyces cerevisiae
brenda