Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme

Catalytic mechanisms of enzymes are well understood, but achieving diverse reaction chemistries in re-engineered proteins can be difficult. Here the authors show a highly efficient and thermostable artificial enzyme that catalyzes a diverse array of substrate oxidations coupled to the reduction of H...

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Autores principales: Daniel W. Watkins, Jonathan M. X. Jenkins, Katie J. Grayson, Nicola Wood, Jack W. Steventon, Kristian K. Le Vay, Matthew I. Goodwin, Anna S. Mullen, Henry J. Bailey, Matthew P. Crump, Fraser MacMillan, Adrian J. Mulholland, Gus Cameron, Richard B. Sessions, Stephen Mann, J. L. Ross Anderson
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/872155373e0341fa822353dc3be89d1d
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Sumario:Catalytic mechanisms of enzymes are well understood, but achieving diverse reaction chemistries in re-engineered proteins can be difficult. Here the authors show a highly efficient and thermostable artificial enzyme that catalyzes a diverse array of substrate oxidations coupled to the reduction of H2O2.