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 | 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 | 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0AF18 | - |
- |
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 | 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 | 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 | Comment | Organism |
---|---|---|
N-acetylglucosamine-6-phosphate deacetylase | - |
Escherichia coli |
NAGPase | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Escherichia coli |