Substrate Dynamics Contribute to Enzymatic Specificity in Human and Bacterial Methionine Adenosyltransferases

[Image: see text] Protein conformational changes can facilitate the binding of noncognate substrates and underlying promiscuous activities. However, the contribution of substrate conformational dynamics to this process is comparatively poorly understood. Here, we analyze human (hMAT2A) and Escherich...

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Detalles Bibliográficos
Autores principales: Gade, Madhuri, Tan, Li Lynn, Damry, Adam M., Sandhu, Mahakaran, Brock, Joseph S., Delaney, Andie, Villar-Briones, Alejandro, Jackson, Colin J., Laurino, Paola
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2021
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8715544/
https://www.ncbi.nlm.nih.gov/pubmed/34977903
http://dx.doi.org/10.1021/jacsau.1c00464

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8715544/
https://www.ncbi.nlm.nih.gov/pubmed/34977903
http://dx.doi.org/10.1021/jacsau.1c00464

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