Any feedback?
Literature summary for 2.6.1.16 extracted from
- Active site-directed inactivation of Escherichia coli glucosamine-6-phosphate synthase. Determination of the fructose 6-phosphate binding constant using a carbohydrate-based inactivator (1996), J. Biol. Chem., 271, 3052-3057.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 2-Amino-2-deoxyglucitol 6-phosphate | competitive with respect to D-fructose 6-phosphate | Escherichia coli |  |
| N-iodoacetylglucosamine 6-phosphate | D-fructose 6-phosphate protects | Escherichia coli | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
3000 Hfr strain (ATCC25257) | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.24 | - |
- |
Escherichia coli |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0193 | - |
2-Amino-2-deoxyglucitol 6-phosphate | pH 7.5, 25°C | 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
