ArticleApplied and environmental microbiology2022
Engineering Isopropanol Dehydrogenase for Efficient Regeneration of Nicotinamide Cofactors.
Article in Applied and environmental microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 44 citations in OpenAlex.
- Improving Activity and Stability of Candida boidinii Formate Dehydrogenase Through Rational Active Site Engineering.Chembiochem : a European journal of chemical biology · 2026Article
- Monooxygenase-dehydrogenase cascade for sustained enzymatic remediation of TMA in salmon protein hydrolysates.Applied and environmental microbiology · 2026Article
- ADP-ribose is a competitive inhibitor of methanol dehydrogenases from Bacillus methanolicus.The Journal of biological chemistry · 2025Article
- Reversible enzyme-catalysed NADChemical science · 2025Article
- Cofactor recycling strategies for secondary metabolite production in cell-free protein expression systems.Biophysical reviews · 2024Review
- Evolving ω-amine transaminaseApplied and environmental microbiology · 2024Article
- Influence of deep eutectic solvents on redox biocatalysis involving alcohol dehydrogenases.Heliyon · 2024Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Isopropanol dehydrogenase (IPADH) is one of the most attractive options for nicotinamide cofactor regeneration due to its low cost and simple downstream processing. However, poor thermostability and strict cofactor dependency hinder its practical application for bioconversions. In this study, we simultaneously improved the thermostability (433-fold) and catalytic activity (3.3-fold) of IPADH from Brucella suis via a flexible segment engineering strategy. Meanwhile, the cofactor preference of IPADH was successfully switched from NAD(H) to NADP(H) by 1.23 × 10
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Registered trials
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