Literature summary for 2.1.1.6 extracted from

Garcia-Meseguer, R.; Zinovjev, K.; Roca, M.; Ruiz-Pernia, J.J.; Tunon, I.
Linking electrostatic effects and protein motions in enzymatic catalysis. A theoretical analysis of catechol O-methyltransferase (2015), J. Phys. Chem. B, 119, 873-882.

Crystallization (Commentary)

Crystallization (Comment)	Organism
quantum mechanics/molecular mechanics computational analysis of catechol O-methylation in aqueous solution and in the active site. A large fraction of the environmental motions needed to attain the transition state happens during the first stages of the reaction. The incorporation of the solvent coordinate in the definition of the transition state improves the transmission coefficient and the committor histogram in solution, while the changes are much less significant in the enzyme. The equilibrium solvation approach seems then to work better in the enzyme than in aqueous solution because the enzyme provides a preorganized environment where the reaction takes place	Rattus norvegicus

Crystallization (Comment)

Organism

quantum mechanics/molecular mechanics computational analysis of catechol O-methylation in aqueous solution and in the active site. A large fraction of the environmental motions needed to attain the transition state happens during the first stages of the reaction. The incorporation of the solvent coordinate in the definition of the transition state improves the transmission coefficient and the committor histogram in solution, while the changes are much less significant in the enzyme. The equilibrium solvation approach seems then to work better in the enzyme than in aqueous solution because the enzyme provides a preorganized environment where the reaction takes place

Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	P22734	-	-

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Release 2023.1 (January 2023)