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Literature summary extracted from

  • Laine-Cessac, P.; Allain, P.
    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.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.35 K+ most effective monovalent cation in activation. Improves both affinity for the substrates and maximal velocity. Km: 35 mM Homo sapiens
2.7.1.35 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
2.7.1.35 Na+ increases maximal velocity and affinity for ATP, but decreases affinity for pyridoxal Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.35 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.1.35 erythrocyte
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.35 ATP + pyridoxal
-
 Homo sapiens ADP + pyridoxal 5'-phosphate
-
 ?