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Literature summary for 2.7.1.35 extracted from
- Kinetic studies of the effects of K+, Na+, and Li+ on the catalytic activity of human erythrocyte pyridoxal kinase (1997), Enzyme Protein, 49, 291-304.
Metals/Ions
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| erythrocyte | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + pyridoxal | - |
Homo sapiens | ADP + pyridoxal 5'-phosphate | - |
? | |
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