The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli

Biochem J. 1967 Oct;105(1):121-5. doi: 10.1042/bj1050121.


1. N-Acetylglucosamine 6-phosphate deacetylase and 2-amino-2-deoxy-d-glucose 6-phosphate ketol-isomerase (deaminating) (EC, glucosamine 6-phosphate deaminase) of Escherichia coliK(12) have been separated by chromatography on DEAE-cellulose. 2. N-Acetylglucosamine 6-phosphate deacetylase has optimum pH8.5 and K(m) 0.8mm. Glucosamine 6-phosphate is a product of the reaction. There appear to be no essential cofactors. Glucosamine 6-phosphate and fructose 6-phosphate inhibit deacetylation. 3. Glucosamine 6-phosphate deaminase has optimum pH7.0 and K(m) 9.0mm. It is stimulated by N-acetylglucosamine 6-phosphate. 4. We propose that the deacetylase be termed 2-acetamido-2-deoxy-d-glucose 6-phosphate amidohydrolase (EC 3.5.1.-), with acetylglucosamine 6-phosphate deacetylase as a trivial name.

MeSH terms

  • Cellulose
  • Chemical Precipitation
  • Chromatography, Ion Exchange
  • Escherichia coli / enzymology*
  • Hydrogen-Ion Concentration
  • Isomerases / analysis*
  • Kinetics
  • Models, Biological
  • Stimulation, Chemical


  • Cellulose
  • Isomerases