8J3P
Formate dehydrogenase mutant from from Candida dubliniensis M4 complexed with NADP+
Summary for 8J3P
| Entry DOI | 10.2210/pdb8j3p/pdb |
| Descriptor | Formate dehydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
| Functional Keywords | formate dehydrogenase, complex, nadp+, oxidoreductase |
| Biological source | Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841) (Yeast) |
| Total number of polymer chains | 3 |
| Total formula weight | 129583.94 |
| Authors | Ma, W.,Zheng, Y.C.,Geng, Q.,Chen, C.,Xu, J.H. (deposition date: 2023-04-17, release date: 2023-09-20, Last modification date: 2023-11-01) |
| Primary citation | Ma, W.,Geng, Q.,Chen, C.,Zheng, Y.C.,Yu, H.L.,Xu, J.H. Engineering a Formate Dehydrogenase for NADPH Regeneration. Chembiochem, 24:e202300390-e202300390, 2023 Cited by PubMed Abstract: Nicotinamide adenine dinucleotide (NADH) and nicotinamide adenine dinucleotide phosphate (NADPH) constitute major hydrogen donors for oxidative/reductive bio-transformations. NAD(P)H regeneration systems coupled with formate dehydrogenases (FDHs) represent a dreamful method. However, most of the native FDHs are NAD -dependent and suffer from insufficient reactivity compared to other enzymatic tools, such as glucose dehydrogenase. An efficient and competitive NADP -utilizing FDH necessitates the availability and robustness of NADPH regeneration systems. Herein, we report the engineering of a new FDH from Candida dubliniensis (CdFDH), which showed no strict NAD preference by a structure-guided rational/semi-rational design. A combinatorial mutant CdFDH-M4 (D197Q/Y198R/Q199N/A372S/K371T/▵Q375/K167R/H16L/K159R) exhibited 75-fold intensification of catalytic efficiency (k /K ). Moreover, CdFDH-M4 has been successfully employed in diverse asymmetric oxidative/reductive processes with cofactor total turnover numbers (TTNs) ranging from 135 to 986, making it potentially useful for NADPH-required biocatalytic transformations. PubMed: 37455264DOI: 10.1002/cbic.202300390 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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