Most enzymatic reactions have very large and remarkably similar apparent second-order
rate constants, kcat/KM, at mean values of about 107 M-1 s-1 with kcat in the range of 10 …

Some half-century ago Pauling (1, 2) proposed that the lowering of the activation energy in
enzyme catalysis stems from the enzyme's affinity for the transition state exceeding it's …

Binding TS in preference to S and increasing TΔ S‡ by freezing out motions in E⊙ S and
E⊙ TS have been accepted as the driving forces in enzymatic catalysis; however, the …

Reactions within enzyme-substrate (E ‚S) complexes share with intramolecular reactions the
close proximity of reactants. This proximity effect results in a much larger numerical value of …

The hydrolytic haloalkane dehalogenases are promising bioremediation and biocatalytic
agents. Two general classes of dehalogenases have been reported from Xanthobacter and …

With the growing acceptance of the contribution of protein conformational ensembles to
enzyme catalysis and regulation, research in the field of protein dynamics has shifted toward …

Structural comparison of three different haloalkane dehalogenases suggested that substrate
specificity of these bacterial enzymes could be significantly influenced by the size and shape …

Enzymes are widely used for the synthesis of pharmaceuticals, agrochemicals, and food
additives because they can catalyze enantioselective transformations.[1] Understanding the …

The steric effect, exerted by enzymes on their reacting substrates, has been considered as a
major factor in enzyme catalysis. In particular, it has been proposed that enzymes catalyze …

Lately, there has been great interest in performing free-energy perturbation (FEP) at the
combined quantum mechanics and molecular mechanics (QM/MM) level, eg for enzyme …