Characterization of an Aldehyde Oxidoreductase From the Mesophilic Bacterium Aromatoleum aromaticum EbN1, a Member of a New Subfamily of Tungsten-Containing Enzymes.

ABSTRACT: The biochemical properties of a new tungsten-containing aldehyde oxidoreductase from the mesophilic betaproteobacterium Aromatoleum aromaticum EbN1 (AOR _Aa ) are presented in this study. The enzyme was purified from phenylalanine-grown cells of an overexpressing mutant lacking the gene for an aldehyde dehydrogenase normally involved in anaerobic phenylalanine degradation. AOR _Aa catalyzes the oxidation of a broad variety of aldehydes to the respective acids with either viologen dyes or NAD⁺ as electron acceptors. In contrast to previously known AORs, AOR _Aa is a heterohexameric protein consisting of three different subunits, a large subunit containing the W-cofactor and an Fe-S cluster, a small subunit containing four

SUBMITTER: Arndt F 

PROVIDER: S-EPMC6365974 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature