ArticleProceedings of the National Academy of Sciences of the United States of America2001
Substrate conformational transitions in the active site of chorismate mutase: their role in the catalytic mechanism.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 97 citations in OpenAlex.
- AcceleratingThe journal of physical chemistry. B · 2022Article
- Restricting the ψ Torsion Angle Has Stereoelectronic Consequences on a Scissile Bond: An Electronic Structure Analysis.Biochemistry · 2015Article
- 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
- Article
- Transition-state charge stabilization through multiple non-covalent interactions in the guanidinium-catalyzed enantioselective Claisen rearrangement.Journal of the American Chemical Society · 2011Article
- Article
- A dynamic view of enzyme catalysis.Journal of molecular modeling · 2008Article
- How similar are enzyme active site geometries derived from quantum mechanical theozymes to crystal structures of enzyme-inhibitor complexes? Implications for enzyme design.Protein science : a publication of the Protein Society · 2007Article
- Chemical accuracy in QM/MM calculations on enzyme-catalysed reactions.Chemistry Central journal · 2007Article
- Correct and incorrect nucleotide incorporation pathways in DNA polymerase beta.Biochemical and biophysical research communications · 2006Article
- The proficiency of a thermophilic chorismate mutase enzyme is solely through an entropic advantage in the enzyme reaction.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Interaction-dependent gene expression in Mla-specified response to barley powdery mildew.The Plant cell · 2004Article
- Extended molecular dynamics simulation of the carbon monoxide migration in sperm whale myoglobin.Biophysical journal · 2004Article
- The mechanism of catalysis of the chorismate to prephenate reaction by the Escherichia coli mutase enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Chorismate mutase acts at the first branch-point of aromatic amino acid biosynthesis and catalyzes the conversion of chorismate to prephenate. The results of molecular dynamics simulations of the substrate in solution and in the active site of chorismate mutase are reported. Two nonreactive conformers of chorismate are found to be more stable than the reactive pseudodiaxial chair conformer in solution. It is shown by QM/MM molecular dynamics simulations, which take into account the motions of the enzyme, that when these inactive conformers are bound to the active site, they are rapidly converted to the reactive chair conformer. This result suggests that one contribution of the enzyme is to bind the more prevalent nonreactive conformers and transform them into the active form in a step before the chemical reaction. The motion of the reactive chair conformer in the active site calculated by using the QM/MM potential generates transient structures that are closer to the transition state than is the stable CHAIR conformer.
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