Purification and Characterization of Pyridoxal 4-Dehydrogenase from Aureobacterium luteolum

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A pyridoxal dehydrogenase was purified to homogeneity from Aureobacterium luteolum, which can use pyridoxine as a carbon and nitrogen source, and characterized. The enzyme was a dimeric protein with a subunit molecular weight of 38,000. It had several properties distinct from those of the partially purified enzyme from Pseudomonas MA-1. The optimum pH (8.0-8.5) was 0.8-1.3 lower than that of the Pseudomonas enzyme. The Aureobacterium enzyme showed much higher and lower affinities for NAD^+ (Km, 0.140 ± 0.008 mM) and pyridoxal (0.473 ± 0.109 mM), respectively, than those of the Pseudomonas enzyme. The Aureobacterium enzyme could use NADP^+ as a substrate : the reactivity was 6.5% of NAD^+. The enzyme was much more tolerant to metal-chelating agents. Irreversibility of the enzymatic reaction was shared by the two enzymes. No aldehyde dehydrogenase showed similarity to the amino-terminal amino acid sequence of the enzyme.
社団法人日本農芸化学会の論文
2002-03-23