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Literature summary extracted from
- Tight binding inhibitors of N-acyl amino sugar and N-acyl amino acid deacetylases (2006), J. Am. Chem. Soc., 128, 4244-4245.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.1.25 | methyl phosphonamidates inhibitor 1 | tetrahedral reaction intermediate analogues | Escherichia coli |  |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.1.25 | Zn2+ | 1 equivalent of zinc bound at the Mbeta site, the enzyme contains a binuclear metal center at the active site | 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 | - |
D-glucosamine 6-phosphate + acetate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.5.1.25 | Escherichia coli | - |
gene nagA | - |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.5.1.25 | N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate + acetate | catalytic mechanism, enzyme-substrate interaction analysis | 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 | - |
Escherichia coli | D-glucosamine 6-phosphate + acetate | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.5.1.25 | NagA | - |
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 |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.5.1.25 | additional information | - |
additional information | inhibition kinetics, inhibitor binding model | Escherichia coli | |
| 3.5.1.25 | 0.000034 | - |
methyl phosphonamidates inhibitor 1 | pH 7.5, 30°C, recombinant enzyme | Escherichia coli | |
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Release 2023.1 (January 2023)
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