Purification and characterization of N-acetylglucosamine 6-phosphate deacetylase with activity against N-acetylglucosamine from Vibrio cholerae non-O1

Biosci Biotechnol Biochem. 1996 Aug;60(8):1320-3. doi: 10.1271/bbb.60.1320.


An enzyme that deacetylates N-acetylglucosamine to glucosamine from Vibrio cholerae non-O1 was purified to homogeneity by sequential procedures. The native enzyme had a molecular mass of 190,000 Da and was predicted to be composed of four identical subunits with molecular masses of 45,000 Da. The purified enzyme hydrolyzed N-acetylglucosamine, N-acetylglucosamine 6-phosphate, and N-acetylglucosamine 6-sulfate, but not chitin oligosaccharides, and N-acetylgalactosamine. The deacetylase activity was completely abolished by N-ethylmaleimide, p-chloromercuribenzoate, EDTA, and Cu2+. On the other hand, the activity was activated by Co2+. The amino-terminal amino acids of the purified enzyme were sequenced. Among the 22 N-terminal amino acid residues, 12 residues of Vibrio deacetylase were identical with that of Escherichia coli GlcNAc 6-phosphate deacetylase.

MeSH terms

  • Acetylglucosamine / chemistry*
  • Amidohydrolases / antagonists & inhibitors
  • Amidohydrolases / chemistry
  • Amidohydrolases / isolation & purification*
  • Amino Acid Sequence
  • Hydrogen-Ion Concentration
  • Metals / chemistry
  • Molecular Sequence Data
  • Sequence Homology, Amino Acid
  • Substrate Specificity
  • Temperature
  • Vibrio cholerae / enzymology*


  • Metals
  • Amidohydrolases
  • N-acetylglucosamine-6-phosphate deacetylase
  • Acetylglucosamine