ArticleProceedings of the National Academy of Sciences of the United States of America2002
The mechanism of catalysis of the chorismate to prephenate reaction by the Escherichia coli mutase enzyme.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 57 citations in OpenAlex.
- Mechanism of the Stereoselective Catalysis of Diels-Alderase PyrE3 Involved in Pyrroindomycin Biosynthesis.Journal of the American Chemical Society · 2022Article
- Quantum chemical modeling of the reaction path of chorismate mutase based on the experimental substrate/product complex.FEBS open bio · 2017Article
- Interdomain Conformational Changes Provide Allosteric Regulation en Route to Chorismate.The Journal of biological chemistry · 2016Article
- Methyltransferases do not work by compression, cratic, or desolvation effects, but by electrostatic preorganization.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
- Modification of residue 42 of the active site loop with a lysine-mimetic side chain rescues isochorismate-pyruvate lyase activity in Pseudomonas aeruginosa PchB.Biochemistry · 2012Article
- Pericyclic reactions catalyzed by chorismate-utilizing enzymes.Biochemistry · 2011Review
- pH Dependence of catalysis by Pseudomonas aeruginosa isochorismate-pyruvate lyase: implications for transition state stabilization and the role of lysine 42.Biochemistry · 2011Article
- Entropic and enthalpic components of catalysis in the mutase and lyase activities of Pseudomonas aeruginosa PchB.Journal of the American Chemical Society · 2011Article
- Examining the case for the effect of barrier compression on tunneling, vibrationally enhanced catalysis, catalytic entropy and related issues.FEBS letters · 2010Review
- A dynamic view of enzyme catalysis.Journal of molecular modeling · 2008Article
- The near attack conformation approach to the study of the chorismate to prephenate reaction.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Molecular dynamics studies of the Escherichia coli chorismate mutase (EcCM), containing at the active site chorismate and in turn the transition state (TS), have been performed. The simulations show that TS is not bound any tighter than chorismate. Comparison of average polar interactions show they are virtually identical for interactions of EcCM with chorismate and the TS, whereas hydrophobic interactions with TS are much weaker than with chorismate. Interactions and the mechanism of catalysis of chorismate --> prephenate by the EcCM enzyme are discussed.
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