Literature DB >> 28190624

Thermodynamic Activity-Based Interpretation of Enzyme Kinetics.

Jürgen Pleiss1.   

Abstract

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. For a solvent-independent analysis of substrate specificity, the thermodynamic activity of the substrate, rather than its concentration, must be considered.
Copyright © 2017 Elsevier Ltd. All rights reserved.

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Year:  2017        PMID： 28190624     DOI： 10.1016/j.tibtech.2017.01.003

Source DB:  PubMed          Journal:  Trends Biotechnol        ISSN： 0167-7799            Impact factor:   19.536


  2 in total

1.  Combined Linear Interaction Energy and Alchemical Solvation Free-Energy Approach for Protein-Binding Affinity Computation.

Authors:  Eko Aditya Rifai; Valerio Ferrario; Jürgen Pleiss; Daan P Geerke
Journal:  J Chem Theory Comput       Date:  2020-01-21       Impact factor: 6.006

2.  Thermodynamics and Kinetics of Glycolytic Reactions. Part I: Kinetic Modeling Based on Irreversible Thermodynamics and Validation by Calorimetry.

Authors:  Kristina Vogel; Thorsten Greinert; Monique Reichard; Christoph Held; Hauke Harms; Thomas Maskow
Journal:  Int J Mol Sci       Date:  2020-11-06       Impact factor: 5.923
  2 in total

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