Cargando…
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...
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: | |
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 |
Ejemplares similares
-
The Role of Salt Bridges, Charge Density, and Subunit Flexibility in Determining Disassembly Routes of Protein Complexes
por: Hall, Zoe, et al.
Publicado: (2013) -
An intermolecular salt bridge linking substrate binding and P1 substrate specificity switch of arterivirus 3C-like proteases
por: Chen, Qian, et al.
Publicado: (2022) -
Sarpagan bridge enzyme has substrate-controlled cyclization and aromatization modes
por: Dang, Thu-Thuy T, et al.
Publicado: (2018) -
Entropic contribution to enhanced thermal stability in the thermostable P450 CYP119
por: Liu, Zhuo, et al.
Publicado: (2018) -
Inverting the Regioselectivity of the Berberine Bridge Enzyme by Employing Customized Fluorine-Containing Substrates
por: Resch, Verena, et al.
Publicado: (2012)