Defects in the acd gene (which may be allelic to ubiH) result in the inactivation of the coenzyme A-linked acetaldehyde dehydrogenase activity of the multifunctional AdhE protein of Escherichia coli. This activity is restored by addition of ubiquinone-0 to cell extracts. However, the alcohol dehydrogenase activity of the AdhE protein is not decreased by an acd mutation. Abolition of ubiquinone biosynthesis by mutation of ubiA or ubiF does not affect either the acetaldehyde dehydrogenase or the alcohol dehydrogenase activity of AdhE. Guaiacol (2-methoxyphenol), which resembles the intermediate that builds up in ubiH mutants, except in lacking the octaprenyl side-chain, was found to inhibit ethanol metabolism in vivo, presumably via inhibition of acetaldehyde dehydrogenase. In vitro assays confirmed that guaiacol inhibited acetaldehyde dehydrogenase. This suggests that the acetaldehyde dehydrogenase activity of AdhE is specifically inhibited by intermediates of ubiquinone synthesis that accumulate in acd mutants and that this inhibition may be relieved by ubiquinone. Copyright (C) 2000 Federation of European Microbiological Societies.
Gupta, S., Mat-Jan, F., Latifi, M., & Clark, D. P. (2000). Acetaldehyde dehydrogenase activity of the AdhE protein of Escherichia coli is inhibited by intermediates in ubiquinone synthesis. FEMS Microbiology Letters, 182(1), 51–55. https://doi.org/10.1016/S0378-1097(99)00568-6