Abstract
Aldehyde dehydrogenase, isolated from the luminescent bacterium, Vibrio harveyi, catalyzes the oxidation of fatty aldehydes (Meighen et al.,1976). This enzyme has a preference for long chain aldehydes as reflected by a large decrease in the Km for aldehydes on increasing the chain length from acetaldehyde to tetradecanal (Bognar & Meighen, 1978; Vedadi et al., 1995). As one of the substrates for luciferase is tetradecanal, the potential involvement of aldehyde dehydrogenase in the luminescent system has been proposed. Tetradecanal is produced in luminescent bacteria by a lux-specific fatty acid reductase complex which activates (plus ATP) tetradecanoic acid to fatty acyl-AMP; the acyl group is then transferred between the fatty acid reductase subunits before being reduced with NADPH (Riendeau et al., 1982; Rodriguez et al., 1983a, 1983b). The V. harveyi aldehyde dehydrogenase(Vh ALDH) may be present so as to maintain aldehyde at nontoxic levels under conditions where excess levels of aldehyde are produced by the fatty acid reductase complex. However, the possibility that the function of aldehyde dehydrogenase is unrelated to luminescence can certainly not be excluded as Vh ALDH is under different regulation than the lux-specific proteins and has not been detected in other luminescent bacteria (Byers et al., 1988; Vedadi, M. unpublished data).
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Vedadi, M., Croteau, N., Delarge, M., Vrielink, A., Meighen, E. (1996). Structural and Functional Studies of A NADP+-Specific Aldehyde Dehydrogenase from the Luminescent Marine Bacterium Vibrio harveyi . In: Weiner, H., Lindahl, R., Crabb, D.W., Flynn, T.G. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 6. Advances in Experimental Medicine and Biology, vol 414. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5871-2_31
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