Secondary Alcohol Dehydrogenases from Thermoanaerobacter pseudoethanolicus and Thermoanaerobacter brockii as Robust Catalysts. (8th April 2021)

• Record Type: Journal Article
• Authors: Musa, Musa M.; Vieille, Claire; Phillips, Robert S.
• Is Part Of: Chembiochem. Volume 22:Number 11(2021)
• Page Start: 1884
• Page End: 1893
• Publication Date: 2021-04-08
• Subjects: alcohol dehydrogenases -- optically active alcohols -- protein engineering -- redox reactions -- TeSADH -- TbSADH; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.202100043
• Languages: English
• ISSNs: 1439-4227

Abstract

Abstract: Alcohol dehydrogenases (ADHs) are an important type of enzyme that have significant applications as biocatalysts. Secondary ADHs from Thermoanaerobacter pseudoethanolicus ( Te SADH) and Thermoanaerobacter brockii ( Tb SADH) are well‐known as robust catalysts. However, like most other ADHs, these enzymes suffer from their high substrate specificities (i. e., limited substrate scope), which to some extent restricts their use as biocatalysts. This minireview discusses recent efforts to expand the substrate scope and tune the enantioselectivity of Te SADH and Tb SADH by using site‐directed mutagenesis and directed evolution. Various examples of asymmetric synthesis of optically active alcohols using both enzymes are highlighted. Moreover, the unique thermal stability and organic solvent tolerance of these enzymes is illustrated by their concurrent inclusion with other interesting reactions to synthesize optically active alcohols and amines. For instance, Te SADH has been used in quantitative non‐stereoselective oxidation of alcohols to deracemize alcohols via cyclic deracemization and in the racemization of enantiopure alcohols to accomplish a bienzymatic dynamic kinetic resolution. Abstract : Scope and selectivity : Recent efforts to expand the substrate scope and tune the enantioselectivity of secondary ADHs from T. pseudoethanolicus and T. brockii by using site‐directed mutagenesis and directed evolution are reviewed. Moreover, the thermal stability and organic solvent tolerance of these enzymes is illustrated by their concurrent inclusion in other interesting reactions to produce optically active alcohols and amines.