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. 1967 Oct;105(1):121–125. doi: 10.1042/bj1050121

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

R J White 1, C A Pasternak 1
PMCID: PMC1198282  PMID: 4861885

Abstract

1. 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 Escherichia coli K12 have been separated by chromatography on DEAE-cellulose. 2. N-Acetylglucosamine 6-phosphate deacetylase has optimum pH8·5 and Km 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 Km 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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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