The only enzyme demonstrated so far to catalyze the formation of 4-pyridoxic
acid, the final excretory product of vitamin B(6), was aldehyde oxidase. In this paper we
have presented an evidence that another enzyme, NAD^+-dependent aldehyde dehydrogenase,
is capable of catalyzing this reaction.
Rat mutants with high, low and no aldehyde oxidase activity excrete the same amount
of isotope after a single injection of ³H-pyridoxol in a 12-day experiment; 4-pyridoxic acid
is also present in the urine of animals without aldehyde oxidase activity. There is no correlation
between the proportion of the excreted acid and the amount of pyridoxal excreted,
after the injection of a single dose of the aldehyde form. The K(m) values for pyridoxal and
NAD^+, at pH 9.6, have been found to be 75 and 260 μmol/1, respectively. NAD^+-dependent
pyridoxal dehydrogenase was partially purified from the rat tissues, and the following
specific enzyme activities (nmol·min^-1·mg^-1 protein) were found: red blood cell 71.5±3.0,
intestine 64.9 ±9.0, muscle 61.4 ±1.6, brain 39.5 ±6.0, liver 34.4 ±3.3, kidney 21.1 ±5.6,
heart 18.8±0.9, and lung 6.5±2.0. This is believed to be the first report demonstrating
pyridoxal oxidation, catalyzed by an NAD^+-dependent aldehyde dehydrogenase.