Enzymatic catalysis of the peptidyl-prolyl bond rotation:: Are transition state formation and enzyme dynamics directly linked?

The search for the answer to the question posed in the title has been helped by results by Eisenmesser et al. on the cyclophilin 18-catalyzed peptidyl-prolyl cis/trans isomerization. Here their results are discussed in connection with previously published data about the catalytic mechanism of this enzyme class. For several of the amino acid side chains (see picture) present in the active center of the enzyme it could be shown that they are involved in substrate binding or in formation of the transition state.