NADP-dependent isopropanol dehydrogenase

NADP-dependent isopropanol dehydrogenase is an enzyme that catalyzes the reversible oxidation of isopropanol (propan-2-ol) to acetone, using NADP+ as an electron acceptor and generating NADPH and a proton[1][5][6]. It primarily acts on medium-chain secondary alcohols with low activity for primary alcohols; it can also reduce aldehydes and 2-ketones to the corresponding secondary alcohols[1][5]. The enzyme belongs to the oxidoreductase family, specifically the alcohol dehydrogenases acting on the CH-OH group of donors with NADP+ as cofactor. It is of particular interest in industrial biotechnology for biocatalysis and metabolic engineering aimed at renewable production of acetone, isopropanol, and the regeneration of cofactors (NADPH) in bioprocesses[6][1]. Human therapeutic targeting of this enzyme is not established, and its principal applications are in microbial or enzymatic biotransformations. It is also identified by EC number 1.1.1.80 and has been studied in organisms such as Thermoanaerobacter brockii and engineered strains of bacteria[1][5][6].

Other names

isopropanol dehydrogenase (NADP+)EC 1.1.1.80propan-2-ol:NADP+ oxidoreductase1.1.1.80

Catalyzes reversible oxidation-reduction of isopropanol and acetone via NADP+ reduction to NADPH, typically in microorganisms or engineered organisms[1][5][6]