Occurrence of N-acetylglucosamine-1-phosphate in proteinase I from Dictyostelium discoideum.
A previous study (Gustafson, G.L., and Thon, L. A. (1979) Biochem. Biophys. Res. Commun. 86, 667-673) demonstrated that Proteinase I from the cellular slime mold, Dictyostelium discoideum, was conjugated with phosphoryl moieties. This report describes a characterization of the covalent structure of these moieties. Essentially all of the phosphate associated with purified enzyme was released as a sugar-phosphate during mild alkaline hydrolysis. The sugar-phosphate was isolated from alkaline hydrolysates of Proteinase I by Sephadex G-25 chromatography and identified as the alpha-anomer of N-acetylglucosamine-1-phosphate. In separate experiments, involving acid hydrolysis of Proteinase I, it was shown that enzyme-phosphate could also be isolated as O-phosphorylserine. Based on the recovery of O-phosphorylserine from acid hydrolysates, it was concluded that the majority of the N-acetylglucosamine-1-phosphate residues in the proteinase were esterified to peptidyl serines through phosphoester bonds.
D000117:Acetylglucosamine / Q000031:analogs & derivatives / Q000032:analysis*; D004023:Dictyostelium / Q000201:enzymology*; D010450:Endopeptidases; D005944:Glucosamine / Q000031:analogs & derivatives*; D005958:Glucosephosphates / Q000032:analysis*; D010750:Phosphoproteins; D010768:Phosphoserine / Q000032:analysis; D011485:Protein Binding; D012697:Serine Endopeptidases
D005958:Glucosephosphates; D010750:Phosphoproteins; D010768:Phosphoserine; C026146:N-acetylglucosamine-1-phosphate; D010450:Endopeptidases; C025097:Escherichia coli periplasmic proteinase; D012697:Serine Endopeptidases; D005944:Glucosamine; D000117:Acetylglucosamine