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iron-containing alcohol dehydrogenase
iron-containing alcohol dehydrogenase catalyzes the iron-dependent reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P) to NAD(P)H; similar to lactaldehyde reductase which catalyzes the interconversion between L-lactaldehyde and L-1,2-propanediol
lactaldehyde reductase
This clade of genes encoding iron-containing alcohol dehydrogenase (PF00465) proteins is generally found in apparent operons for the catabolism of rhamnose or fucose. Catabolism of both of these monosaccharides results in lactaldehyde which is reduced by this enzyme to 1,2 propanediol [1]. This protein is alternatively known by the name 1,2 propanediol oxidoreductase. This enzyme is active under anaerobic conditions in E. coli while being inactivated by reactive oxygen species under aerobic conditions [2]. Under aerobic conditions the lactaldehyde product of rhamnose and fucose catabolism is believed to be oxidized to lactate by a separate enzyme, lactaldehyde dehydrogenase.
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