Isolation and some properties of NAD-linked 2-carboxybenzaldehyde dehydrogenase in Alcaligenes faecalis AFK 2 grown on phenanthrene.

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Abstract
An NAD-linked 2-carboxybenzaldehyde dehydrogenase which catalyzes the conversion of 2-carboxybenzaldehyde to o-phthalate was isolated and purified about 130-fold from the cell extract of A. faecalis AFK2 which was grown on phenanthrene. The purified enzyme had MW of .apprx. 160,000, and consisted of 4 molecules of a single kind of polypeptide having a MW of 40,000. It showed high specificity for 2-carboxybenzaldehyde as its substrate and for NAD as its electron acceptor. The Km values for the substrate and NAD were 5.4 .times. 10-5 and 1.4 .times. 10-4 M, respectively. Because of the increase in the enzym level by the growth on phenanthrene, the enzyme was inducible, suggesting its responsibility for the degradation of phenanthrene in A. faecalis AFK2.