Any feedback?
Literature summary extracted from
- N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion (2007), Biochemistry, 46, 7942-7952.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.5.1.25 | - |
Escherichia coli |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.5.1.25 | 0.08 | - |
N-acetyl-D-glucosamine 6-phosphate | - |
Escherichia coli |  |
| 3.5.1.25 | 0.08 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant Q59A | Escherichia coli | |
| 3.5.1.25 | 0.1 | - |
N-acetyl-D-glucosamine 6-phosphate | Zn in acitve site changed to Mn | Escherichia coli | |
| 3.5.1.25 | 0.15 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant E131A | Escherichia coli | |
| 3.5.1.25 | 0.15 | - |
N-acetyl-D-glucosamine 6-phosphate | Zn in acitve site changed to Co | Escherichia coli | |
| 3.5.1.25 | 0.2 | - |
N-acetyl-D-glucosamine 6-phosphate | Zn in acitve site changed to Cd | Escherichia coli | |
| 3.5.1.25 | 0.2 | - |
N-thioacetyl-D-glucosamine 6-phosphate | Zn in acitve site changed to Cd | Escherichia coli | |
| 3.5.1.25 | 0.23 | - |
N-acetyl-D-glucosamine 6-phosphate | Zn in acitve site changed to Fe | Escherichia coli | |
| 3.5.1.25 | 0.23 | - |
N-thioacetyl-D-glucosamine 6-phosphate | Zn in acitve site changed to Mn | Escherichia coli | |
| 3.5.1.25 | 0.24 | - |
N-thioacetyl-D-glucosamine 6-phosphate | - |
Escherichia coli | |
| 3.5.1.25 | 0.29 | - |
N-formyl-D-glucosamine 6-phosphate | - |
Escherichia coli | |
| 3.5.1.25 | 0.31 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant Q59H | Escherichia coli | |
| 3.5.1.25 | 0.33 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant H143Q | Escherichia coli | |
| 3.5.1.25 | 0.4 | - |
N-trifluoroacetyl-D-glucosamine 6-phosphate | - |
Escherichia coli | |
| 3.5.1.25 | 0.64 | - |
N-acetyl-D-glucosamine 6-phosphate | Zn in acitve site changed to Ni | Escherichia coli | |
| 3.5.1.25 | 0.76 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant Y223F | Escherichia coli | |
| 3.5.1.25 | 0.8 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant N61A | Escherichia coli | |
| 3.5.1.25 | 1.24 | - |
N-Acetyl-D-galactosamine 6-phosphate | - |
Escherichia coli | |
| 3.5.1.25 | 1.7 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant N61H | Escherichia coli | |
| 3.5.1.25 | 2 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant K139M | Escherichia coli | |
| 3.5.1.25 | 2.1 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant H143N | Escherichia coli | |
| 3.5.1.25 | 2.7 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant H251N | Escherichia coli | |
| 3.5.1.25 | 3.6 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant E131Q | Escherichia coli | |
| 3.5.1.25 | 4.9 | - |
N-acetyl-D-glucosamine 6-sulfate | - |
Escherichia coli | |
| 3.5.1.25 | 11 | - |
N-acetyl-D-glucosamine 6-sulfate | Zn in acitve site changed to Cd | Escherichia coli | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.1.25 | Zn | one cation per subunit | Escherichia coli | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.25 | 180000 | - |
- |
Escherichia coli |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.5.1.25 | Escherichia coli | P0AF18 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.5.1.25 | anion exchange column | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.1.25 | N-acetyl-D-galactosamine 6-phosphate + H2O | - |
Escherichia coli | D-galactosamine 6-phosphate + acetate | - |
? | |
| 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-sulfate + H2O | - |
Escherichia coli | D-glucosamine 6-sulfate + acetate | - |
? | |
| 3.5.1.25 | N-formyl-D-glucosamine 6-phosphate + H2O | - |
Escherichia coli | D-glucosamine 6-phosphate + formate | - |
? | |
| 3.5.1.25 | N-thioacetyl-D-glucosamine 6-phosphate + H2O | - |
Escherichia coli | D-glucosamine 6-phosphate + thioacetate | - |
? | |
| 3.5.1.25 | N-trifluoroacetyl-D-glucosamine 6-phosphate + H2O | - |
Escherichia coli | D-glucosamine 6-phosphate + trifluoroacetate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.5.1.25 | tetramer | - |
Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.5.1.25 | N-acetyl-D-glucosamine-6-phosphate deacetylase | - |
Escherichia coli |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.5.1.25 | 0.02 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant D273A | Escherichia coli | |
| 3.5.1.25 | 0.02 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant D273N | Escherichia coli | |
| 3.5.1.25 | 0.43 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant H143N | Escherichia coli | |
| 3.5.1.25 | 0.7 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant E131Q | Escherichia coli | |
| 3.5.1.25 | 1.9 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant E131A | Escherichia coli | |
| 3.5.1.25 | 2.4 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant H143Q | Escherichia coli | |
| 3.5.1.25 | 2.6 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant N61H | Escherichia coli | |
| 3.5.1.25 | 6.8 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant H251N | Escherichia coli | |
| 3.5.1.25 | 10 | - |
N-thioacetyl-D-glucosamine 6-phosphate | - |
Escherichia coli | |
| 3.5.1.25 | 10 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant Q59A | Escherichia coli | |
| 3.5.1.25 | 11 | - |
N-thioacetyl-D-glucosamine 6-phosphate | Zn in acitve site changed to Mn | Escherichia coli | |
| 3.5.1.25 | 22 | - |
N-formyl-D-glucosamine 6-phosphate | - |
Escherichia coli | |
| 3.5.1.25 | 23 | - |
N-acetyl-D-glucosamine 6-sulfate | Zn in acitve site changed to Cd | Escherichia coli | |
| 3.5.1.25 | 24 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant N61A | Escherichia coli | |
| 3.5.1.25 | 32 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant Q59H | Escherichia coli | |
| 3.5.1.25 | 35 | - |
N-acetyl-D-glucosamine 6-phosphate | enzyme with 0.4 eqivalents of Zn per subunit bound | Escherichia coli | |
| 3.5.1.25 | 41 | - |
N-acetyl-D-glucosamine 6-phosphate | Zn in acitve site changed to Ni | Escherichia coli | |
| 3.5.1.25 | 49 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant K139M | Escherichia coli | |
| 3.5.1.25 | 58 | - |
N-acetyl-D-glucosamine 6-phosphate | Zn in acitve site changed to Fe | Escherichia coli | |
| 3.5.1.25 | 64 | - |
N-acetyl-D-glucosamine 6-sulfate | - |
Escherichia coli | |
| 3.5.1.25 | 92 | - |
N-acetyl-D-glucosamine 6-phosphate | Zn in acitve site changed to Mn | Escherichia coli | |
| 3.5.1.25 | 96 | - |
N-acetyl-D-glucosamine 6-phosphate | enzyme with 1 equivalent of Zn per subunit bound | Escherichia coli | |
| 3.5.1.25 | 128 | - |
N-thioacetyl-D-glucosamine 6-phosphate | Zn in acitve site changed to Cd | Escherichia coli | |
| 3.5.1.25 | 154 | - |
N-Acetyl-D-galactosamine 6-phosphate | - |
Escherichia coli | |
| 3.5.1.25 | 163 | - |
N-acetyl-D-glucosamine 6-phosphate | Zn in acitve site changed to Cd | Escherichia coli | |
| 3.5.1.25 | 167 | - |
N-acetyl-D-glucosamine 6-phosphate | mutant Y223F | Escherichia coli | |
| 3.5.1.25 | 177 | - |
N-acetyl-D-glucosamine 6-phosphate | Zn in acitve site changed to Co | Escherichia coli | |
| 3.5.1.25 | 2610 | - |
N-trifluoroacetyl-D-glucosamine 6-phosphate | - |
Escherichia coli | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
