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Quantum chemical modeling of the reaction path of chorismate mutase based on the experimental substrate/product complex

Content Provider	Scilit
Author	Burschowsky, Daniel Krengel, Ute Uggerud, Einar Balcells, David
Copyright Year	2017
Description	Journal: FEBS Open Bio Chorismate mutase is a well‐known model enzyme, catalyzing the Claisen rearrangement of chorismate to prephenate. Recent high‐resolution crystal structures along the reaction coordinate of this enzyme enabled computational analyses at unprecedented detail. Using quantum chemical simulations, we investigated how the catalytic reaction mechanism is affected by electrostatic and hydrogen‐bond interactions. Our calculations showed that the transition state (TS) was mainly stabilized electrostatically, with Arg90 playing the leading role. The effect was augmented by selective hydrogen‐bond formation to the TS in the wild‐type enzyme, facilitated by a small‐scale local induced fit. We further identified a previously underappreciated water molecule, which separates the negative charges during the reaction. The analysis includes the wild‐type enzyme and a non‐natural enzyme variant, where the catalytic arginine was replaced with an isosteric citrulline residue.
Related Links	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5458464/pdf
Ending Page	797
Page Count	9
Starting Page	789
ISSN	22115463
e-ISSN	22115463
DOI	10.1002/2211-5463.12224
Journal	FEBS Open Bio
Issue Number	6
Volume Number	7
Language	English
Publisher	Wiley-Blackwell
Publisher Date	2017-05-02
Access Restriction	Open
Subject Keyword	Journal: FEBS Open Bio Biochemistry and Molecular Biology Chorismate Mutase Claisen Rearrangement Enzyme Catalysis Pericyclic Reaction Transition State Stabilization
Content Type	Text
Resource Type	Article
Subject	Biochemistry, Genetics and Molecular Biology

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Chorismate-mutase-catalyzed claisen rearrangement.

Transition state stabilization and substrate strain in enzyme catalysis: ab initio QM/MM modelling of the chorismate mutase reaction

Mechanistic studies of an antibody with chorismate mutase activity.

The effect of MM polarization on the QM/MM transition state stabilization: application to chorismate mutase

A novel noncovalent complex of chorismate mutase and DAHP synthase from Mycobacterium tuberculosis: protein purification, crystallization and X-ray diffraction analysis.

Enzymes do what is expected (chalcone isomerase versus chorismate mutase) (2002).

High-accuracy computation of reaction barriers in enzymes

Electrostatic transition state stabilization rather than reactant destabilization provides the chemical basis for efficient chorismate mutase catalysis

Comparison of formation of reactive conformers (NACs) for the Claisen rearrangement of chorismate to prephenate in water and in the E. coli mutase: the efficiency of the enzyme catalysis.

Quantum chemical modeling of the reaction path of chorismate mutase based on the experimental substrate/product complex

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Transition state stabilization and substrate strain in enzyme catalysis: ab initio QM/MM modelling of the chorismate mutase reaction

Mechanistic studies of an antibody with chorismate mutase activity.

The effect of MM polarization on the QM/MM transition state stabilization: application to chorismate mutase

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Quantum chemical modeling of the reaction path of chorismate mutase based on the experimental substrate/product complex