8j3o

Formate dehydrogenase wild-type enzyme from Candida dubliniensis complexed with NADH

spinqualitylabelsall models 8j3o, resolution 2.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8j3o is a 4 chain structure with sequence from Candida dubliniensis CD36. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.65Å Ligands: MG, NAI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B9WHT3_CANDC Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms.[HAMAP-Rule:MF_03210] Publication Abstract from PubMed 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/triangle upQ375/K167R/H16L/K159R) exhibited 75-fold intensification of catalytic efficiency (k(cat) /K(m) ). 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. Engineering a Formate Dehydrogenase for NADPH Regeneration.,Ma W, Geng Q, Chen C, Zheng YC, Yu HL, Xu JH Chembiochem. 2023 Jul 16:e202300390. doi: 10.1002/cbic.202300390. PMID:37455264 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA