Purification and Characterization of N-Acetylglucosamine 6-Phosphate Deacetylase with Activity against N-Acetylglucosamine from Vibrio cholerae Non-O1.

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  • Purification and Characterization of<i>N</i>-Acetylglucosamine 6-Phosphate Deacetylase with Activity against<i>N</i>-Acetylglucosamine from<i>Vibrio cholerae</i>Non-O1
  • Purification and characterization of N-acetylglucosamine 6-phosphate deacetylase with activity against N-acetylglucosamine from Vibrio cholerae non-01

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An enzyme that doacetylates 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.

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