Purification and Characterization of a Dehydrogenase Catalyzing Conversion of Nα-Benzyloxycarbonyl-L-Aminoadipic-δ-Semialdehyde to Nα-Benzyloxycarbonyl-L-Aminoadipic Acid from Rhodococcus sp. AIU Z-35-1

The enzyme catalyzing conversion of Nα-benzyloxycarbonyl-L-aminoadipic-δ-semialdehyde (Nα-Z-L-AASA) to Nα-benzyloxycarbonyl-L-aminoadipic acid (Nα-Z-L-AAA) in Rhodococcus sp. AIU Z-35-1 was identified, and its characteristics were revealed. This reaction was catalyzed by a dehydrogenase with a molecular mass of 59 kDa. The dehydrogenase exhibited enzyme activity on not only Nα-Z-L-AASA but also Nα-Z-D-AASA and short chain aliphatic aldehydes, but not on aromatic aldehydes and alcohols. The apparent Km values for Nα-Z-L-AASA, Nα-Z-D-AASA and NAD+ were estimated to be 3.8 mM, 14.1 mM and 0.16 mM, respectively. The NH2 terminal amino acid sequence of this enzyme exhibited a similarity to those of a piperidein-6-carboxylate dehydrogenase from Streptomyces clavuligerus and a putative dehydrogenase from Rhodococcus sp. RHA 1, but not to those of other microbial aldehyde dehydrogenases.