1887

Abstract

, a Gram-positive soil bacterium belonging to the actinomycetes, is able to degrade formaldehyde but the enzyme(s) involved in this detoxification process were not known. Acetaldehyde dehydrogenase Ald, which is essential for ethanol utilization, and FadH, characterized here as NAD-linked mycothiol-dependent formaldehyde dehydrogenase, were shown to be responsible for formaldehyde oxidation since a mutant lacking and could not oxidize formaldehyde resulting in the inability to grow when formaldehyde was added to the medium. Moreover, ΔΔ did not grow with vanillate, a carbon source giving rise to intracellular formaldehyde. FadH from was purified from recombinant and shown to be active as a homotetramer. Mycothiol-dependent formaldehyde oxidation revealed values of 0.6 mM for mycothiol and 4.3 mM for formaldehyde and a of 7.7 U mg. FadH from also possesses zinc-dependent, but mycothiol-independent alcohol dehydrogenase activity with a preference for short chain primary alcohols such as ethanol (  = 330 mM,  = 9.6 U mg), 1-propanol (  = 150 mM,  = 5 U mg) and 1-butanol (  = 50 mM,  = 0.8 U mg). Formaldehyde detoxification system by Ald and mycothiol-dependent FadH is essential for tolerance of to external stress by free formaldehyde in its habitat and for growth with natural substrates like vanillate, which are metabolized with concomitant release of formaldehyde.

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2013-12-01
2021-10-27
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