7QUL

Alcohol Dehydrogenase from Thauera aromatica K319A/K320A mutant

Summary for 7QUL

• Entry DOI: 10.2210/pdb7qul/pdb
• Descriptor: 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase, 1,2-ETHANEDIOL, ZINC ION, ... (4 entities in total)
• Functional Keywords: alcohol dehydrogenase, ketoreductase, nadh, oxidoreductase
• Biological source: Thauera aromatica
• Total number of polymer chains: 1
• Total formula weight: 37343.45

Authors

Petchey, M.L.,Stark, F.,Ansorge-Schumacher, M.,Grogan, G. (deposition date: 2022-01-18, release date: 2022-08-17, Last modification date: 2024-01-31)

Primary citation

Stark, F.,Loderer, C.,Petchey, M.,Grogan, G.,Ansorge-Schumacher, M.B.
Advanced Insights into Catalytic and Structural Features of the Zinc-Dependent Alcohol Dehydrogenase from Thauera aromatica.
Chembiochem, 23:e202200149-e202200149, 2022

PubMed 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.

PubMed: 35557486
DOI: 10.1002/cbic.202200149

Experimental method

X-RAY DIFFRACTION (1.8 Å)