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Literature summary extracted from

  • White, R.J.; Pasternak, C.A.
    N-Acetylglucosamine-6-phosphate deacetylase and glucosamine-6-phosphate deaminase from Escherichia coli (1975), Methods Enzymol., 41, 497-502.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.25 fructose-6-phosphate
-
Escherichia coli
3.5.1.25 glucosamine 6-phosphate mixed type inhibition Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.25 Bacillus subtilis
-
-
-
3.5.1.25 Bifidobacterium bifidum
-
var. pennsylvanicus
-
3.5.1.25 Bos taurus
-
-
-
3.5.1.25 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.25
-
Escherichia coli

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.1.25 parotid gland
-
Bos taurus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.5.1.25 5.6
-
-
Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.25 N-acetyl-D-glucosamine 6-phosphate + H2O
-
Bacillus subtilis D-glucosamine 6-phosphate + acetate
-
?
3.5.1.25 N-acetyl-D-glucosamine 6-phosphate + H2O
-
Escherichia coli D-glucosamine 6-phosphate + acetate
-
ir
3.5.1.25 N-acetyl-D-glucosamine 6-phosphate + H2O
-
Bos taurus D-glucosamine 6-phosphate + acetate
-
?
3.5.1.25 N-acetyl-D-glucosamine 6-phosphate + H2O
-
Bifidobacterium bifidum D-glucosamine 6-phosphate + acetate
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.25 8.5
-
-
Escherichia coli