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Literature summary for 3.5.1.25 extracted from

  • White, R.J.; Pasternak, C.A.
    The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli (1967), Biochem. J., 105, 121-125.
    View publication on PubMedView publication on EuropePMC

General Stability

General Stability Organism
prolonged dialysis against 10 mM sodium phosphate buffer, pH 7.0, causes little loss of activity Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
acetate no inhibition Escherichia coli
fructose-6-phosphate
-
Escherichia coli
glucosamine 6-phosphate
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.8
-
N-acetyl-D-glucosamine 6-phosphate
-
Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
K12
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
56
-
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-D-glucosamine 6-phosphate + H2O
-
Escherichia coli D-glucosamine 6-phosphate + acetate
-
ir

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
7 9 pH 7.0: about 45% of maximal activity, pH 9.0: about 55% of maximal activity Escherichia coli