7qul
From Proteopedia
Alcohol Dehydrogenase from Thauera aromatica K319A/K320A mutant
Structural highlights
FunctionHAD_THAAR Involved in the central benzoyl-CoA catabolism. Catalyzes the oxidation of 6-hydroxycyclohex-1-ene-1-carbonyl-CoA to 6-oxocyclohex-1-ene-1-carbonyl-CoA. It is specific to NAD and is also able to oxidize 2-hydroxycyclohexane-1-carbonyl-CoA.[1] [2] Publication Abstract from PubMedThe 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 alpha-diketone 1,2-cyclohexanedione to the corresponding alpha-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 alpha-substituted cyclohexanones, and indicated structural determinants responsible for the unique substrate acceptance. Advanced Insights into Catalytic and Structural Features of the Zinc-Dependent Alcohol Dehydrogenase from Thauera aromatica.,Stark F, Loderer C, Petchey M, Grogan G, Ansorge-Schumacher MB Chembiochem. 2022 Aug 3;23(15):e202200149. doi: 10.1002/cbic.202200149. Epub 2022, Jun 14. PMID:35557486[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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