Crystallization and properties of NADP-dependent aldehyde dehydrogenase from Gluconobacter melanogenus.

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Abstract
NADP-dependent aldehyde dehydrogenase (EC 1.2.1.4) has been crystallized for the first time from cytosol fraction of Gluconobacter melanogenus IFO 3293. Purification of the enzyme was performed by column chromatographies on DEAE-Sephadex A-50 and hydroxylapatite. The enzyme was purified about 60-fold with an overall yield of 33%. Crystalline enzyme was found homogeneous in disc gel electrophoresis and analytical ultracentrifugation. The enzyme was highly specific for NADP and completely inactive with NAD. Abundance of the enzyme in cytosol fraction and its predominant occurrence through acetic acid bacteria indicated the importance of the enzyme in ethanol assimilation. NADPH formed in aldehyde oxidation was reoxidized into NADP by the old yellow enzyme system which existed in the same cytosol fraction of the organism. Cyclic regeneration of NADP smoothly occurred in the presence of acetaldehyde dehydrogenase, old yellow enzyme and catalase, even when a limited amount of NADP or NADPH was present in the reaction mixture.

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