title: Protein motions and dynamic effects in enzyme catalysis.
abstract: The role of protein motions in promoting the chemical step of enzyme catalysed reactions remains a subject of considerable debate. Here, a unified view of the role of protein dynamics in dihydrofolate reductase catalysis is described. Recently the role of such motions has been investigated by characterising the biophysical properties of isotopically substituted enzymes through a combination of experimental and computational analyses. Together with previous work, these results suggest that dynamic coupling to the chemical coordinate is detrimental to catalysis and may have been selected against during DHFR evolution. The full catalytic power of Nature's catalysts appears to depend on finely tuning protein motions in each step of the catalytic cycle.
authors: School of Chemistry, Cardiff University, Park Place, Cardiff, CF10 3AT, UK. allemannrk@cardiff.ac.uk.
authors: Louis Y P
authors: LY
authors: Luk
authors: School of Chemistry, Cardiff University, Park Place, Cardiff, CF10 3AT, UK. allemannrk@cardiff.ac.uk.
authors: E Joel
authors: EJ
authors: Loveridge
authors: School of Chemistry, Cardiff University, Park Place, Cardiff, CF10 3AT, UK. allemannrk@cardiff.ac.uk.
authors: Rudolf K
authors: RK
authors: Allemann
mesh_terms: D055162:Biocatalysis; D020134:Catalytic Domain; D004926:Escherichia coli / Q000201:enzymology* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D016297:Mutagenesis, Site-Directed; D012997:Solvents / Q000737:chemistry; D013762:Tetrahydrofolate Dehydrogenase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D029968:Escherichia coli Proteins; D012997:Solvents; D013762:Tetrahydrofolate Dehydrogenase