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Literature summary for 3.5.1.25 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)

Crystallization (Comment) Organism
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

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

Metals/Ions

Metals/Ions Comment Organism Structure
additional information enzyme inactivation by metal-sequestering agents and subsequent reactivation by the addition of several divalent cations Escherichia coli
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)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AF18
-
-

Reaction

Reaction Comment Organism Reaction ID
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

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

Subunits

Subunits Comment Organism
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

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

Temperature Optimum [°C]

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

pH Optimum

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