Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
K+ | most effective monovalent cation in activation. Improves both affinity for the substrates and maximal velocity. Km: 35 mM | Homo sapiens | |
Li+ | poor activator which seems to modify the enzymatic mechanism from a random to an ordered sequential pattern with ATP bound before pyridoxal. Km: 37 mM | Homo sapiens | |
Na+ | increases maximal velocity and affinity for ATP, but decreases affinity for pyridoxal | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
erythrocyte | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + pyridoxal | - |
Homo sapiens | ADP + pyridoxal 5'-phosphate | - |
? |