Ground-State Destabilization by Active-Site Hydrophobicity Controls the Selectivity of a Cofactor-Free Decarboxylase

[Image: see text] Bacterial arylmalonate decarboxylase (AMDase) and evolved variants have become a valuable tool with which to access both enantiomers of a broad range of chiral arylaliphatic acids with high optical purity. Yet, the molecular principles responsible for the substrate scope, activity,...

Descripción completa

Detalles Bibliográficos
Autores principales: Biler, Michal, Crean, Rory M., Schweiger, Anna K., Kourist, Robert, Kamerlin, Shina Caroline Lynn
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2020
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7735706/
https://www.ncbi.nlm.nih.gov/pubmed/33180505
http://dx.doi.org/10.1021/jacs.0c10701

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7735706/
https://www.ncbi.nlm.nih.gov/pubmed/33180505
http://dx.doi.org/10.1021/jacs.0c10701

Ejemplares similares