ENZYMATIC STUDIES ON PYRIDOXINE METABOLISM:IV. A PYRIDOXINE DEHYDROGENASE FROM BAKER'S YEAST

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Description

1. Pyridoxine dehydrogenase from baker's yeast was purified about 80-fold over crude extracts.<br> 2. The enzyme required TPN ; DPN was not effective.<br> 3. The reaction seems to favor the reduction of pyridoxal.<br> 4. The optimum pH for this enzyme was pH 9.3.<br> 5. The enzymatic activity was stimulated by Co++ and Mg++<br> 6. The enzyme activity was inhibited by p-CMB. The inhibition by p-CMB was prevented by preincubation of the apoenzyme with TPN and reversed by the addition of reduced glutathione.<br> 7. This enzyme seems to be concerned with the oxido-reduction reaction between the hydroxymethyl group and the formyl group at position 4 of pyridine ring.<br> 8. The distribution of pyridoxine dehydrogenase was examined.<br> 9. A possible action mechanism for B6-antagonists such as 5-deoxypyridoxine and 5-deoxypyridoxal is discussed.

Journal

  • J Biochem (Tokyo)

    J Biochem (Tokyo) 48 (5), 733-744, 1960

    The Japanese Biochemical Society

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