Abstract
The substrate activity of pyridoxamine (PM) for brain pyridoxal (PL) kinase was examined in view of a recent report which indicated that PM was a poor substrate for this enzyme. Bovine brain PL kinase was shown by liquid chromatography to catalyze the phosphorylation of PM (Km = 65 microM). The identity of the reaction product, pyridoxamine 5'-phosphate, was confirmed by is ability to act as a substrate for liver pyridoxine (pyridoxamine) 5'-phosphate oxidase. The results, which indicate that PM is a good substrate for brain PL kinase, are consistent with the proposed role of intracellular phosphorylation in the uptake of vitamin B-6 brain tissue.
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