Occurrence of N-acetylglucosamine-1-phosphate in proteinase I from Dictyostelium discoideum

J Biol Chem. 1980 Aug 10;255(15):7208-10.


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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetylglucosamine / analogs & derivatives
  • Acetylglucosamine / analysis*
  • Dictyostelium / enzymology*
  • Endopeptidases*
  • Glucosamine / analogs & derivatives*
  • Glucosephosphates / analysis*
  • Phosphoproteins
  • Phosphoserine / analysis
  • Protein Binding
  • Serine Endopeptidases*


  • Glucosephosphates
  • Phosphoproteins
  • Phosphoserine
  • N-acetylglucosamine-1-phosphate
  • Endopeptidases
  • Escherichia coli periplasmic proteinase
  • Serine Endopeptidases
  • Glucosamine
  • Acetylglucosamine