ArticleProceedings of the National Academy of Sciences of the United States of America2008
On the relationship between folding and chemical landscapes in enzyme catalysis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Methods for the establishment of enzymatic mechanisms - from QM to ML.Chemical science · 2026Review
- Perspective: Defining and quantifying the role of dynamics in enzyme catalysis.The Journal of chemical physics · 2016Review
- Recent advances in QM/MM free energy calculations using reference potentials.Biochimica et biophysica acta · 2015Review
- Conformational heterogeneity and intrinsic disorder in enzyme regulation: Glucokinase as a case study.Intrinsically disordered proteins · 2015Article
- Electrostatic transition state stabilization rather than reactant destabilization provides the chemical basis for efficient chorismate mutase catalysis.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Measurement of histidine pKa values and tautomer populations in invisible protein states.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Exploration of swapping enzymatic function between two proteins: a simulation study of chorismate mutase and isochorismate pyruvate lyase.Protein science : a publication of the Protein Society · 2013Article
- Conformational effects on the pro-S hydrogen abstraction reaction in cyclooxygenase-1: an integrated QM/MM and MD study.Biophysical journal · 2013Article
- Hydrogen tunneling links protein dynamics to enzyme catalysis.Annual review of biochemistry · 2013Review
- Molecular dynamics simulation of the last step of a catalytic cycle: product release from the active site of the enzyme chorismate mutase from Mycobacterium tuberculosis.Protein science : a publication of the Protein Society · 2012Article
- Paradynamics: an effective and reliable model for ab initio QM/MM free-energy calculations and related tasks.The journal of physical chemistry. B · 2011Article
- Multiscale modeling of biological functions.Physical chemistry chemical physics : PCCP · 2011Review
- Stochastic ensembles, conformationally adaptive teamwork, and enzymatic detoxification.Biochemistry · 2011Article
- Update 1 of: Tunneling and dynamics in enzymatic hydride transfer.Chemical reviews · 2010Article
- Impact of oxidation on protein therapeutics: conformational dynamics of intact and oxidized acid-β-glucocerebrosidase at near-physiological pH.Protein science : a publication of the Protein Society · 2010Article
- Elucidation of the conformational free energy landscape in H.pylori LuxS and its implications to catalysis.BMC structural biology · 2010Article
- Examining the case for the effect of barrier compression on tunneling, vibrationally enhanced catalysis, catalytic entropy and related issues.FEBS letters · 2010Review
- An Analysis of All the Relevant Facts and Arguments Indicates that Enzyme Catalysis Does Not Involve Large Contributions from Nuclear Tunneling.Journal of physical organic chemistry · 2010Article
- At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis?Proteins · 2010Review
- Multiscale simulations of protein landscapes: using coarse-grained models as reference potentials to full explicit models.Proteins · 2010Article
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4 authors.
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Abstract
Elucidating the relationship between the folding landscape of enzymes and their catalytic power has been one of the challenges of modern enzymology. The present work explores this issue by using a simplified folding model to generate the free-energy landscape of an enzyme and then to evaluate the activation barriers for the chemical step in different regions of the landscape. This approach is used to investigate the recent finding that an engineered monomeric chorismate mutase exhibits catalytic efficiency similar to the naturally occurring dimer even though it exhibits the properties of an intrinsically disordered molten globule. It is found that the monomer becomes more confined than its native-like counterpart upon ligand binding but still retains a wider catalytic region. Although the overall rate acceleration is still determined by reduction of the reorganization energy, the detailed contribution of different barriers yields a more complex picture for the chemical process than that of a single path. This work provides insight into the relationship between folding landscapes and catalysis. The computational approach used here may also provide a powerful strategy for modeling single-molecule experiments and designing enzymes.
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