Cargando…
Chemical Ligation and Isotope Labeling to Locate Dynamic Effects during Catalysis by Dihydrofolate Reductase
Chemical ligation has been used to alter motions in specific regions of dihydrofolate reductase from E. coli and to investigate the effects of localized motional changes on enzyme catalysis. Two isotopic hybrids were prepared; one with the mobile N‐terminal segment containing heavy isotopes ((2)H, (...
Autores principales: | Luk, Louis Y. P., Ruiz‐Pernía, J. Javier, Adesina, Aduragbemi S., Loveridge, E. Joel, Tuñón, Iñaki, Moliner, Vincent, Allemann, Rudolf K. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
WILEY‐VCH Verlag
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4985705/ https://www.ncbi.nlm.nih.gov/pubmed/26079622 http://dx.doi.org/10.1002/anie.201503968 |
Ejemplares similares
-
Why Are Some Enzymes Dimers? Flexibility and Catalysis
in Thermotoga maritima Dihydrofolate Reductase
por: Ruiz-Pernía, J. Javier, et al.
Publicado: (2019) -
Minimization of dynamic effects in the evolution of dihydrofolate reductase
por: Ruiz-Pernía, J. Javier, et al.
Publicado: (2016) -
Loss of Hyperconjugative Effects Drives Hydride Transfer
during Dihydrofolate Reductase Catalysis
por: Angelastro, Antonio, et al.
Publicado: (2019) -
Electric Field Measurements Reveal the Pivotal Role
of Cofactor–Substrate Interaction in Dihydrofolate Reductase
Catalysis
por: Adesina, Aduragbemi S., et al.
Publicado: (2020) -
Increased
Dynamic Effects in a Catalytically Compromised
Variant of Escherichia coli Dihydrofolate Reductase
por: Ruiz-Pernia, J. Javier, et al.
Publicado: (2013)