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Literature summary extracted from
- A possible mechanism for the in vitro activation of L-serine deaminase activity in Escherichia coli K12 (1990), Biochem. Cell Biol., 68, 723-728.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.3.1.17 | additional information | the enzyme is inactive in crude extract and can be activated with iron and dithiothreitol. The activation requires oxygen, and is inhibited by free radical scavengers and by diethylenentriamine pentaacetic acid, which prevents Fe cycling | Escherichia coli |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.3.1.17 | D-His | - |
Escherichia coli |  |
| 4.3.1.17 | imidazole | - |
Escherichia coli | |
| 4.3.1.17 | L-His | - |
Escherichia coli | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.3.1.17 | Escherichia coli | - |
K12 | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.3.1.17 | L-serine | - |
Escherichia coli | pyruvate + NH3 | - |
? | |
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