Coenzyme Binding Site Analysis of an Isopropanol Dehydrogenase with Wide Substrate Spectrum and Excellent Organic Solvent Tolerance.

NAD(P)H-dependent enzymes are ideal biocatalysts for the industrial production of chiral compounds， such as chiral alcohols， chiral amino acids， and chiral amines; however， efficient strategies for the regeneration of coenzyme are expected as costly of the coenzymes. Herein， a solvent-tolerant isopropanol dehydrogenase (IDH) showing lower similarity (37%) with other proteins was obtained and characterized. The enzyme exhibits high catalysis ability of its substrates methanol， ethanol， ethylene glycol， glycerol， isopropanol， n-butanol， isobutanol， and acetone. And it has good adaptability in organic solvents (isopropanol， acetonitrile， acetone， and acetophenone). Interaction force and the corresponding amino acid residues between IDH and NAD or NADP were parsed by docking. The wide substrate spectrum， excellent organic solvent tolerance， and good biocatalytic activity make the excavated enzyme a promising biocatalyst for the production of chiral compounds industrially and the construction of coenzyme regeneration systems in aqueous organic phase or organic phase.