Cargando…
Different Dynamical Effects in Mesophilic and Hyperthermophilic Dihydrofolate Reductases
[Image: see text] The role of protein dynamics in the reaction catalyzed by dihydrofolate reductase from the hyperthermophile Thermotoga maritima (TmDHFR) has been examined by enzyme isotope substitution ((15)N, (13)C, (2)H). In contrast to all other enzyme reactions investigated previously, includi...
Autores principales: | Luk, Louis Y. P., Loveridge, E. Joel, Allemann, Rudolf K. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2014
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4046772/ https://www.ncbi.nlm.nih.gov/pubmed/24779446 http://dx.doi.org/10.1021/ja502673h |
Ejemplares similares
-
Minimization of dynamic effects in the evolution of dihydrofolate reductase
por: Ruiz-Pernía, J. Javier, et al.
Publicado: (2016) -
Thermal Adaptation of Dihydrofolate Reductase from
the Moderate Thermophile Geobacillus stearothermophilus
por: Guo, Jiannan, et al.
Publicado: (2014) -
Chemical Ligation and Isotope Labeling to Locate Dynamic Effects during Catalysis by Dihydrofolate Reductase
por: Luk, Louis Y. P., et al.
Publicado: (2015) -
Cryo‐kinetics Reveal Dynamic Effects on the Chemistry of Human Dihydrofolate Reductase
por: Adesina, Aduragbemi S., et al.
Publicado: (2021) -
Increased
Dynamic Effects in a Catalytically Compromised
Variant of Escherichia coli Dihydrofolate Reductase
por: Ruiz-Pernia, J. Javier, et al.
Publicado: (2013)