ArticleBiochemistry2016
Structural and Kinetic Studies of Formate Dehydrogenase from Candida boidinii.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Thermally reversible Diels-Alder linkers enable reusable methacrylate supports for enzyme immobilisation.Chemical communications (Cambridge, England) · 2026Article
- Improving Activity and Stability of Candida boidinii Formate Dehydrogenase Through Rational Active Site Engineering.Chembiochem : a European journal of chemical biology · 2026Article
- Semiartificial COChemical reviews · 2026Review
- Detecting Vibrational Energy Transfer into an Enzyme Active Site via a Transition State Analog.The journal of physical chemistry letters · 2026Article
- Formate Dehydrogenase: The Role of the AMP Cofactor Fragment in Stabilization of the Transition State for Enzyme-Catalyzed Hydride Transfer.ACS omega · 2026Article
- Enzyme Architecture: Activation of Phosphite Dehydrogenase-Catalyzed Hydride Transfer by NADBiochemistry · 2025Article
- Immobilization of Thrombin on Agarose-Based Supports for Affinity Tag Removal.Biomacromolecules · 2025Article
- Structural analysis of wild-type and Val120Thr mutant Candida boidinii formate dehydrogenase by X-ray crystallography.Acta crystallographica. Section D, Structural biology · 2023Article
- Structures of the holoenzyme TglHI required for 3-thiaglutamate biosynthesis.Structure (London, England : 1993) · 2023Article
- Utilization of Cofactor Binding Energy for Enzyme Catalysis: Formate Dehydrogenase-Catalyzed Reactions of the Whole NAD Cofactor and Cofactor Pieces.Biochemistry · 2023Article
- Direct Biocatalytic Processes for COMolecules (Basel, Switzerland) · 2023Review
- Engineered repeat proteins as scaffolds to assemble multi-enzyme systems for efficient cell-free biosynthesis.Nature communications · 2023Article
- Efficient production of salvianic acid A from L-dihydroxyphenylalanine through a tri-enzyme cascade.Bioresources and bioprocessing · 2023Article
- Light-driven biocatalytic oxidation.Chemical science · 2022Review
- Improving the Enzymatic Cascade of Reactions for the Reduction of COMolecules (Basel, Switzerland) · 2022Review
- Engineering nonphotosynthetic carbon fixation for production of bioplastics by methanogenic archaea.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Asymmetric Azidation under Hydrogen Bonding Phase-Transfer Catalysis: A Combined Experimental and Computational Study.Journal of the American Chemical Society · 2022Article
- COMethods in molecular biology (Clifton, N.J.) · 2022Article
- Conserved Amino Acid Residues that Affect Structural Stability of Candida boidinii Formate Dehydrogenase.Applied biochemistry and biotechnology · 2021Article
- Effect of Metal Ions on the Activity of Ten NAD-Dependent Formate Dehydrogenases.The protein journal · 2020Article
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Authors and funding
8 authors.
Funding
Abstract
The structure of formate dehydrogenase from Candida boidinii (CbFDH) is of both academic and practical interests. First, this enzyme represents a unique model system for studies on the role of protein dynamics in catalysis, but so far these studies have been limited by the availability of structural information. Second, CbFDH and its mutants can be used in various industrial applications (e.g., CO2 fixation or nicotinamide recycling systems), and the lack of structural information has been a limiting factor in commercial development. Here, we report the crystallization and structural determination of both holo- and apo-CbFDH. The free-energy barrier for the catalyzed reaction was computed and indicates that this structure indeed represents a catalytically competent form of the enzyme. Complementing kinetic examinations demonstrate that the recombinant CbFDH has a well-organized reactive state. Finally, a fortuitous observation has been made: the apoenzyme crystal was obtained under cocrystallization conditions with a saturating concentration of both the cofactor (NAD(+)) and inhibitor (azide), which has a nanomolar dissociation constant. It was found that the fraction of the apoenzyme present in the solution is less than 1.7 × 10(-7) (i.e., the solution is 99.9999% holoenzyme). This is an extreme case where the crystal structure represents an insignificant fraction of the enzyme in solution, and a mechanism rationalizing this phenomenon is presented.
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