Electrostatic basis for enzyme catalysis.

By A. Warshel, P. K. Sharma, Mitsunori Kato, Yun Xiang, Hanbin Liu, M. Olsson. Chemical Reviews, 2006

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Estimating conformational heterogeneity of tryptophan synthase with a template‐based Alphafold2 approach (2022, background): “7,8 However, the importance of conformational flexibility was demonstrated with the design of catalytic antibodies.”
Emerging themes in the computational design of novel enzymes and protein–protein interfaces (2013, background): “…to catalysis: they interact favorably with the reaction transition state [19] and they shield the chemical groups that aid catalysis from water [20], thereby increasing their reactivity; together these mechanisms lower the transition-state free energy in the active site microenvironment…”
Attractive noncovalent interactions in asymmetric catalysis: Links between enzymes and small molecule catalysts (2010, background): “Figure 1).(17) While enzymes are understood to achieve selectivity through transition state stabilization, with the rate of the dominant pathway preferentially accelerated relative to competing reactions, small-molecule chiral catalysts are generally proposed to follow a”
External electric field effects on chemical structure and reactivity (2020, background): “As mentioned in the introduction, the LEFs in enzymes play an important role in many catalytic reactions.(15,36) Already in the 1970s, Warshel(16) suggested that the polarity of the active pockets was an overlooked aspect of enzymatic reactivity.”