Thermodynamic Activity-Based Interpretation of Enzyme Kinetics.
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Summary
The experimentally determined Michaelis constant Km results from a combination of two effects: the recognition of the substrate by the enzyme and the interactions between substrate and solvent.
- Type
- article
- Published
- 2017-05-01
- Cited by
- 22
- References
- 12
- OpenAlex
- https://openalex.org/W2587733587
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:205391896
Keywords
Substrate (aquarium), Michaelis–Menten kinetics, Solvent, Kinetics, Chemistry
References
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- Group‐contribution estimation of activity coefficients in nonideal liquid mixtures
- Propioin synthesis using thiamine diphosphate‐dependent enzymes
- Enzyme-like proteins by computational design
- Thermodynamic activity-based enzyme kinetics : Efficient tool for nonaqueous enzymology
- What can we learn by studying enzymes in non-aqueous media?
- Do organic solvents affect the catalytic properties of lipase? Intrinsic kinetic parameters of lipases in ester hydrolysis and formation in various organic solvents
- Investigation of the carboligase activity of thiamine diphosphate-dependent enzymes using kinetic modeling and NMR spectroscopy
- Incomplete mixing versus clathrate-like structures: A molecular view on hydrophobicity in methanol–water mixtures
- Characterization of benzaldehyde lyase from Pseudomonas fluorescens: A versatile enzyme for asymmetric C-C bond formation.
- Thermodynamics of Bioreactions.
- Thermodynamic activity‐based intrinsic enzyme kinetic sheds light on enzyme–solvent interactions
Cited by
- Enzymatic Production of Biodiesel: Strategies to Overcome Methanol Inactivation
- Crowders and Cosolvents-Major Contributors to the Cellular Milieu and Efficient Means to Counteract Environmental Stresses.
- Thermodynamic Activity-Based Progress Curve Analysis in Enzyme Kinetics.
- Interpretation of cytochrome P450 monooxygenase kinetics by modeling of thermodynamic activity.
- Co-solvent effects on reaction rate and reaction equilibrium of an enzymatic peptide hydrolysis.
- Prediction and Experimental Validation of Co-Solvent Influence on Michaelis Constants: A Thermodynamic Activity-Based Approach.
- Molecular simulations of enzymes under non-natural conditions
- Simultaneous Prediction of Cosolvent Influence on Reaction Equilibrium and Michaelis Constants of Enzyme-Catalyzed Ketone Reductions
- Thermodynamic Activity-Based Solvent Design for Bioreactions.
- Cosolvent and pressure effects on enzyme-catalysed hydrolysis reactions.
- Using Deep Eutectic Solvents to Overcome Limited Substrate Solubility in the Enzymatic Decarboxylation of Bio-Based Phenolic Acids
- Combined co-solvent and pressure effect on kinetics of a peptide hydrolysis: an activity-based approach.
- Combined Linear Interaction Energy and Alchemical Solvation Free-Energy Approach for Protein-Binding Affinity Computation
- Thermodynamics and Kinetics of Glycolytic Reactions. Part I: Kinetic Modeling Based on Irreversible Thermodynamics and Validation by Calorimetry
- Standardized Data, Scalable Documentation, Sustainable Storage – EnzymeML As A Basis For FAIR Data Management In Biocatalysis
- Boosting the kinetic efficiency of formate dehydrogenase by combining the effects of temperature, high pressure and co-solvent mixtures.
- Modeling Enzyme Kinetics: Current Challenges and Future Perspectives for Biocatalysis.
- Rationally Engineered Self-assembling Enzyme Immobilization Keratin Platform Towards Multienzymatic Cascade Reactions
- Effect of ECM nanostructures in decellularized small intestine on differentiation of intestinal epithelial model cells
- Bioreactive Separation Technology: A retrospective and perspective
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