Advanced insights into catalytic and structural features of the zinc-dependent alcohol dehydrogenase from Thauera aromatica
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
Abstract
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.
Details
Original language | English |
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Article number | e202200149 |
Pages (from-to) | e202200149 |
Number of pages | 11 |
Journal | ChemBioChem |
Volume | 23 |
Issue number | 15 |
Publication status | Published - 3 Aug 2022 |
Peer-reviewed | Yes |
External IDs
Scopus | 85131807383 |
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PubMed | 35557486 |
WOS | 000810608000001 |
Mendeley | 570cb98b-e300-3314-8d2f-13553826d1d3 |
ORCID | /0000-0002-2912-546X/work/142238752 |
Keywords
Keywords
- Alcohol Dehydrogenase/chemistry, Catalysis, Ketones/chemistry, Substrate Specificity, Thauera/metabolism, Zinc, structure-activity relationships, oxidoreductases, enzyme catalysis, reduction, biocatalysis