M-Glycogenin, the Protein Moiety of Neurospora crassa Proteoglycogen,

ARIEL GOLDRAIJ; JUAN A CURTINO

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Academic Press, Inc.

Año: 1996 vol. 227 p. 909 - 914

0006-291X

Neurospora crassa proteoglycogen was purified and its protein moiety, M-glycogenin, was released by amylolytic treatment. The released protein was capable of autoglucosylation from UDP-glucose forming glucosyl-a1,4-glucosyl linkage. The kinetics of autoglucosylation suggested an intramolecular mechanism of reaction. M-glycogenin was also able to glucosylate dodecyl-b-maltoside and autoglucosylate, simultaneously and independently. Both auto- and transglucosylation reactions were dependent on Mn2/. Thus, M-glycogenin, which has also been described as the constituent of Escherichia coliproteoglycogen was purified and its protein moiety, M-glycogenin, was released by amylolytic treatment. The released protein was capable of autoglucosylation from UDP-glucose forming glucosyl-a1,4-glucosyl linkage. The kinetics of autoglucosylation suggested an intramolecular mechanism of reaction. M-glycogenin was also able to glucosylate dodecyl-b-maltoside and autoglucosylate, simultaneously and independently. Both auto- and transglucosylation reactions were dependent on Mn2/. Thus, M-glycogenin, which has also been described as the constituent of Escherichia colia1,4-glucosyl linkage. The kinetics of autoglucosylation suggested an intramolecular mechanism of reaction. M-glycogenin was also able to glucosylate dodecyl-b-maltoside and autoglucosylate, simultaneously and independently. Both auto- and transglucosylation reactions were dependent on Mn2/. Thus, M-glycogenin, which has also been described as the constituent of Escherichia colib-maltoside and autoglucosylate, simultaneously and independently. Both auto- and transglucosylation reactions were dependent on Mn2/. Thus, M-glycogenin, which has also been described as the constituent of Escherichia coli2/. Thus, M-glycogenin, which has also been described as the constituent of Escherichia coli proteoglycogen (A. Goldraij and J. A. Curtino, 1993, Biochem. Mol. Biol. Int. 30, 453–458), is a glucosyltransferase that bears similar catalytic properties with mammalian glycogenin. This is the first report on the enzymatic character of the protein constituent of proteoglycogen in primitive organisms, which suggest that the mechanism for the de novo biosynthesis of glycogen was conserved over a very long period of evolution. Biochem. Mol. Biol. Int. 30, 453–458), is a glucosyltransferase that bears similar catalytic properties with mammalian glycogenin. This is the first report on the enzymatic character of the protein constituent of proteoglycogen in primitive organisms, which suggest that the mechanism for the de novo biosynthesis of glycogen was conserved over a very long period of evolution. de novo biosynthesis of glycogen was conserved over a very long period of evolution.