Changing the Electron Acceptor Specificity of Rhodobacter capsulatus Formate Dehydrogenase from NAD+ to NADP+ DOI Open Access
Hemant Kumar, Silke Leimkühler

International Journal of Molecular Sciences, Journal Year: 2023, Volume and Issue: 24(22), P. 16067 - 16067

Published: Nov. 8, 2023

Formate dehydrogenases catalyze the reversible oxidation of formate to carbon dioxide. These enzymes play an important role in CO2 reduction and serve as nicotinamide cofactor recycling enzymes. More recently, CO2-reducing activity dehydrogenases, especially metal-containing has been further explored for efficient atmospheric capture. Here, we investigate binding site dehydrogenase from Rhodobacter capsulatus its specificity toward NAD+ vs. NADP+ reduction. Starting NAD+-specific wild-type RcFDH, key residues were exchanged enable on basis NAD+-bound cryo-EM structure (PDB-ID: 6TG9). It observed that lysine at position 157 (Lys157) β-subunit enzyme is essential NAD+. RcFDH variants had Glu259 either a positively charged or uncharged amino acid additional with NADP+. The FdsBL279R FdsBK276A also showed Kinetic parameters all determined tested able reduce using NADPH electron donor coupled assay phosphite (PTDH), which regenerates NADPH. This makes suitable applications where it can be other use

Language: Английский

Engineering Redox Cofactor Balance for Improved 5-Methyltetrahydrofolate Production in Escherichia coli DOI

Jinning Yang,

Yaokang Wu, Xueqin Lv

et al.

Journal of Agricultural and Food Chemistry, Journal Year: 2024, Volume and Issue: 72(17), P. 9974 - 9983

Published: April 16, 2024

5-Methyltetrahydrofolate (5-MTHF) is the sole active form of folate functioning in human body and widely used as a nutraceutical. Unlike pollution from chemical synthesis, microbial synthesis enables green production 5-MTHF. In this study,

Language: Английский

Citations

2
Deep learning for NAD/NADP cofactor prediction and engineering using transformer attention analysis in enzymes DOI

Jaehyung Kim,

Jihoon Woo,

Joon Young Park

et al.

Metabolic Engineering, Journal Year: 2024, Volume and Issue: unknown

Published: Nov. 1, 2024

Language: Английский

Citations

2
Changing the Electron Acceptor Specificity of Rhodobacter capsulatus Formate Dehydrogenase from NAD+ to NADP+ DOI Open Access
Hemant Kumar, Silke Leimkühler

International Journal of Molecular Sciences, Journal Year: 2023, Volume and Issue: 24(22), P. 16067 - 16067

Published: Nov. 8, 2023

Formate dehydrogenases catalyze the reversible oxidation of formate to carbon dioxide. These enzymes play an important role in CO2 reduction and serve as nicotinamide cofactor recycling enzymes. More recently, CO2-reducing activity dehydrogenases, especially metal-containing has been further explored for efficient atmospheric capture. Here, we investigate binding site dehydrogenase from Rhodobacter capsulatus its specificity toward NAD+ vs. NADP+ reduction. Starting NAD+-specific wild-type RcFDH, key residues were exchanged enable on basis NAD+-bound cryo-EM structure (PDB-ID: 6TG9). It observed that lysine at position 157 (Lys157) β-subunit enzyme is essential NAD+. RcFDH variants had Glu259 either a positively charged or uncharged amino acid additional with NADP+. The FdsBL279R FdsBK276A also showed Kinetic parameters all determined tested able reduce using NADPH electron donor coupled assay phosphite (PTDH), which regenerates NADPH. This makes suitable applications where it can be other use

Language: Английский

Citations

1