Controlling the Substrate Specificity of an Enzyme through Structural Flexibility by Varying the Salt-Bridge Density

Many enzymes, particularly in one single family, with highly conserved structures and folds exhibit rather distinct substrate specificities. The underlying mechanism remains elusive, the resolution of which is of great importance for biochemistry, biophysics, and bioengineering. Here, we performed a...

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Detalles Bibliográficos
Autores principales: Huang, Juan, Xu, Qin, Liu, Zhuo, Jain, Nitin, Tyagi, Madhusudan, Wei, Dong-Qing, Hong, Liang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8470667/
https://www.ncbi.nlm.nih.gov/pubmed/34577164
http://dx.doi.org/10.3390/molecules26185693

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8470667/
https://www.ncbi.nlm.nih.gov/pubmed/34577164
http://dx.doi.org/10.3390/molecules26185693

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