Protein motions and dynamic effects in enzyme catalysis

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 charac...

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Published inPhysical chemistry chemical physics : PCCP Vol. 17; no. 46; pp. 3817 - 3827
Main Authors Luk, Louis Y. P, Loveridge, E. Joel, Allemann, Rudolf K
Format Journal Article
LanguageEnglish
Published England 01.01.2015
Subjects
Biocatalysis
Catalysis
Catalysts
Catalytic Domain
Coupling
Dynamics
Enzymes
Escherichia coli - enzymology
Escherichia coli - metabolism
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - genetics
Escherichia coli Proteins - metabolism
Evolution
Kinetics
Mutagenesis, Site-Directed
Proteins
Solvents - chemistry
Tetrahydrofolate Dehydrogenase - chemistry
Tetrahydrofolate Dehydrogenase - genetics
Tetrahydrofolate Dehydrogenase - metabolism
Tuning
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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. While the full catalytic power of dihydrofolate reductase depends on finely tuning protein motions in each step of the catalytic cycle, dynamic coupling to the actual chemical step is detrimental to catalysis.
AbstractList 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.
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.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.
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. While the full catalytic power of dihydrofolate reductase depends on finely tuning protein motions in each step of the catalytic cycle, dynamic coupling to the actual chemical step is detrimental to catalysis.
Author Luk, Louis Y. P
Allemann, Rudolf K
Loveridge, E. Joel
AuthorAffiliation School of Chemistry
Cardiff University
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  givenname: Louis Y. P
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  givenname: E. Joel
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  givenname: Rudolf K
  surname: Allemann
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/25854702$$D View this record in MEDLINE/PubMed
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Snippet 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...
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SubjectTerms Biocatalysis
Catalysis
Catalysts
Catalytic Domain
Coupling
Dynamics
Enzymes
Escherichia coli - enzymology
Escherichia coli - metabolism
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - genetics
Escherichia coli Proteins - metabolism
Evolution
Kinetics
Mutagenesis, Site-Directed
Proteins
Solvents - chemistry
Tetrahydrofolate Dehydrogenase - chemistry
Tetrahydrofolate Dehydrogenase - genetics
Tetrahydrofolate Dehydrogenase - metabolism
Tuning
Title Protein motions and dynamic effects in enzyme catalysis
URI https://www.ncbi.nlm.nih.gov/pubmed/25854702
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