Abstract
The properties of the pyridoxal kinase of mouse brain were studied and the following results were obtained.1. It was concluded that toxopyrimidine seemed to be phosphorylated by the same phosphokinase as pyridoxal based on the following reasons: the mutual competitive inhibition, the coincidence of the metal requirements, the denaturation effects of heat treatment on the enzyme and the behaviors of inhibitors for both substrates.2. The substrate specificities of the pyridoxal-kinase were investigated and the following results were obtained: (a) The pyridoxal-kinase was able to act on both certain pyridine and pyrimidine derivatives (b) The 2-methyl of the pyrimidine ring was able to be substituted with C2H5 or SCH3 group for CH3 group (c) The 4 position of the pyridine ring was able to be substituted with CH2OH, CH2NH2 or CH3 group for CHO group (d) The compounds without a hydroxymethyl group in the 5 position of the pyridine ring were not phosphorylated at all (such as pyrithioxine) or slightly phosphorylated in such a special case as 5-deoxypyridoxine
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