Akademik Veri Yönetim Sistemi
Biocatalysis and Biotransformation, cilt.39, ss.260-268, 2021 (SCI-Expanded)
© 2020 Informa UK Limited, trading as Taylor & Francis Group.NADPH-dependent oxidoreductases are crucial biocatalysts for the industrial production of chiral compounds. For in situ recycling of required expensive cofactors in this biosynthetic process, NAD(P)+-dependent formate dehydrogenases (FDHs) are wanted to be employed as redox biocatalysts due to their greener and process friendly nature. However, their utilization is limited by their undesired cofactor preference that strongly prone to NAD+ more than NADP+ and catalytic efficiency. To mine NADP+-dependent FDHs in nature by the guidance of bioinformatic tools or re-engineering of their NAD+-dependent equivalents to get an applicable recycler are attractive topics in bioengineering. It can be said that, up to now, the attempts to switch the cofactor preference of the FDHs generally have resulted in NADP+-dependent enzymes that have not to catch the desired catalytic efficiencies or stability. In this review, all studies about the native NADP+-dependent FDHs and also engineered equivalents that reconstructed with different protein engineering approaches for altering the coenzyme specificity are outlined. To switch the coenzyme preference of FDHs or to find the native NADP+-dependent FDHs will be the hot topics in bioengineering until finding a feasible regenerator. Therefore, this study will be a useful guide to get a pathway for designing or discovering novel NADP+-dependent FDHs.