Any feedback?
Literature summary for 4.3.1.19 extracted from
- Allosteric regulation of biosynthetic threonine deaminase from Escherichia coli: effects of isoleucine and valine on active-site ligand binding and catalysis (1995), Arch. Biochem. Biophys., 316, 311-318.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| L-Val | activates | Escherichia coli |  |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ile | - |
Escherichia coli | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
biosynthetic threonine deaminase | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-threonine | - |
Escherichia coli | 2-oxobutanoate + NH3 | - |
? | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | required | 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
