Study on the Pyridoxal Kinase of Mouse Brain

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  • TSUBOSAKA MICHIKO
    Department of Biochemistry, The Jikei University School of Medicine Tokyo
  • MAKINO KATASHI
    Department of Biochemistry, The Jikei University School of Medicine Tokyo

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The properties of the pyridoxal kinase of mouse brain were studied and the following results were obtained.<br>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.<br>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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