EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
4.3.3.7 | (S)-lysine | no significant conformational change between the pyruvate-bound and (S)-lysine-bound enzyme, presence of substrate has substantial effect on the nature of enzyme-inhibitor association, solvent plays a key role in binding of inhibitor | Sinorhizobium meliloti |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.3.3.7 | Sinorhizobium meliloti | Q07607 | L5-30 | - |
4.3.3.7 | Sinorhizobium meliloti L5-30 | Q07607 | L5-30 | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
4.3.3.7 | additional information | - |
titration of (S)-lysine into buffered solutions of MosA protein in the presence or absence of saturating amounts of pyruvate, thermodynamic data for (S)-Lysine binding to MosA protein, non-competitive mechanism with substrate-dependent differences in the energetics of inhibitor binding | Sinorhizobium meliloti |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.3.3.7 | DHDPS | - |
Sinorhizobium meliloti |
4.3.3.7 | MosA protein | - |
Sinorhizobium meliloti |