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Literature summary for 4.3.1.18 extracted from
- Isolation and characterization of catabolite-resistant mutants in the D-serine deaminase system of Escherichia coli K-12 (1975), J. Bacteriol., 121, 1085-1091.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-deoxymethylenephosphonate | can substitute for pyridoxal 5'-phosphate, the enzyme exhibits 35-40% of the activity of the native enzyme | Escherichia coli |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
mutants: in the first class of mutants, enzyme synthesis is completely insensitive to catabolite repression | - |
| Escherichia coli | - |
in the second class of mutants the enzyme is partially insensitive to catabolite repression and catabolite repression is reversed by the addition of cAMP binding protein, the constitutive rate of enzyme synthesis is 4fold higher in all mutants of both classes than in the parent | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-serine | - |
Escherichia coli | pyruvate + NH3 | - |
? | |
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