Advanced insights into catalytic and structural features of the zinc-dependent alcohol dehydrogenase from Thauera aromatica

Research output: Contribution to journalResearch articleContributedpeer-review



The asymmetric reduction of ketones to chiral hydroxyl compounds by alcohol dehydrogenases (ADHs) is an established strategy for the provision of valuable precursors for fine chemicals and pharmaceutics. However, most ADHs favor linear aliphatic and aromatic carbonyl compounds, and suitable biocatalysts with preference for cyclic ketones and diketones are still scarce. Among the few candidates, the alcohol dehydrogenase from Thauera aromatica (ThaADH) stands out with a high activity for the reduction of the cyclic α-diketone 1,2-cyclohexanedione to the corresponding α-hydroxy ketone. This study elucidates catalytic and structural features of the enzyme. ThaADH showed a remarkable thermal and pH stability as well as stability in the presence of polar solvents. A thorough description of the substrate scope combined with the resolution and description of the crystal structure, demonstrated a strong preference of ThaADH for cyclic α-substituted cyclohexanones, and indicated structural determinants responsible for the unique substrate acceptance.


Original languageEnglish
Article numbere202200149
Pages (from-to)e202200149
Number of pages11
Issue number15
Publication statusPublished - 3 Aug 2022

External IDs

Scopus 85131807383
PubMed 35557486
WOS 000810608000001
Mendeley 570cb98b-e300-3314-8d2f-13553826d1d3
ORCID /0000-0002-2912-546X/work/142238752



  • Alcohol Dehydrogenase/chemistry, Catalysis, Ketones/chemistry, Substrate Specificity, Thauera/metabolism, Zinc, structure-activity relationships, oxidoreductases, enzyme catalysis, reduction, biocatalysis