PURIFICATION AND PROPERTIES OF N-ACETYLGLUCOSAMINE 6-PHOSPHATE DEACETYLASE FROM ESCHERICHIA COLI

N-Acetylglucosamine 6-phosphate deacetylase and 2-amino-2-deoxy-D-glucose 6-phosphate ketol-isomerase (deaminating) (EC 5.3.1.10, glucosamine 6-phosphate deaminase) of E. coli K12 were separated by chromatography on DEAE-cellulose. N-Acetylglucosamine 6-phosphate deacetylase has optimum pH 8.5 and Km 0.8 mM, Glucosamine 6-phosphate is a product of the reaction. There appear to be no essential cofactors. Glucosamine 6-phosphate and fructose 6-phosphate inhibit deacetyl-ation. Glucosamine 6-phosphate deaminase has optimum pH 7.0 and Km 9.0 mM. It is stimulated by N-acetylglucosamine 6-phosphate. We propose that the deacetylase be termed 2-acetamido-2-deoxy-D-glucose 6-phosphate amidohydrolase (EC 3.5.1.-), with acetylglucos-amine 6-phosphate deacetylase as a trivial name.