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Literature summary extracted from

  • Ferreira, F.M.; Mendoza-Hernandez, G.; Castaneda-Bueno, M.; Aparicio, R.; Fischer, H.; Calcagno, M.L.; Oliva, G.
    Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli (2006), J. Mol. Biol., 359, 308-321.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.25 purified recombinant enzyme, hanging drop vapour diffusion method, 18°C, precipitant is sodium dihydrogen phosphate, X-ray diffraction structure determination and analysis at 2.0-2.9 A resolution Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.25 1,10-phenanthroline
-
 Escherichia coli
3.5.1.25 EDTA
-
 Escherichia coli
3.5.1.25 additional information enzyme inactivation by metal-sequestering agents and subsequent reactivation by the addition of several divalent cations Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.25 additional information enzyme inactivation by metal-sequestering agents and subsequent reactivation by the addition of several divalent cations Escherichia coli
3.5.1.25 Zn2+ zinc metalloenzyme, Zn2+ is bound to the enzyme, 1.4 Zn2+ per polypeptide chain, the metal binding site also binds a phosphate ion Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.25 N-acetyl-D-glucosamine 6-phosphate + H2O Escherichia coli step in amino sugar catabolism D-glucosamine 6-phosphate + acetate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.25 Escherichia coli P0AF18
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.1.25 N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate + acetate active site structure at the bottom of the alpha-domain cavity, catalytic mechanism Escherichia coli
a

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
-
 Escherichia coli D-glucosamine 6-phosphate + acetate
-
 ?
3.5.1.25 N-acetyl-D-glucosamine 6-phosphate + H2O step in amino sugar catabolism Escherichia coli D-glucosamine 6-phosphate + acetate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.25 tetramer analysis of the dimer-dimer interface, the tertiary and quarternary structure, the apoenzyme shows conformational changes in two loops adjacent to the active site, crystal structure Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.5.1.25 N-acetylglucosamine-6-phosphate deacetylase
-
 Escherichia coli
3.5.1.25 NAGPase
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.25 30
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.25 7.5
-
 assay at Escherichia coli