(1) Institute of Technical Microbiology, Hamburg University of Technology (TUHH), Kasernenstr. 12, D-21073 Hamburg, Germany
* Corresponding author
Living organisms have developed strategies to cope with alcoholic substrates. Due to the manifold appearance of alcoholic compounds, enzymes that are capable of decomposing or processing such molecules have emerged several times during evolution. These proteins are the so-called alcohol dehydrogenases, a group of ubiquitous enzymes that catalyse the interconversion between alcohols and aldehydes or ketones. In addition to several other co-factors that are used by alcohol dehydrogenases, three non-homologous protein families exclusively use NAD(P)/NAD(P)H. Two of the three protein families have been predominantly and extensively studied in animals; this short review focuses on bacterial group III alcohol dehydrogenases and sheds some light on their functionality, distribution and potential biotechnological applications.
In contrast to other NAD(P)-dependent ADHs, there is only little information on group III ADHs, however, recent investigations have shown some promise for some of these enzymes. The continuous evaluation of such biocatalysts will aid in the development of environment friendly approaches for the production of fine chemicals, which could provide an alternative to traditional petrochemical routes.