Discovery of processive catalysis by an exo-hydrolase with a pocket-shaped active site

Substrates associate and products dissociate from enzyme catalytic sites rapidly, which hampers investigations of their trajectories. The high-resolution structure of the native Hordeum exo-hydrolase HvExoI isolated from seedlings reveals that non-covalently trapped glucose forms a stable enzyme-pro...

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Detalles Bibliográficos
Autores principales: Streltsov, Victor A., Luang, Sukanya, Peisley, Alys, Varghese, Joseph N., Ketudat Cairns, James R., Fort, Sebastien, Hijnen, Marcel, Tvaroška, Igor, Ardá, Ana, Jiménez-Barbero, Jesús, Alfonso-Prieto, Mercedes, Rovira, Carme, Mendoza, Fernanda, Tiessler-Sala, Laura, Sánchez-Aparicio, José-Emilio, Rodríguez-Guerra, Jaime, Lluch, José M., Maréchal, Jean-Didier, Masgrau, Laura, Hrmova, Maria
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6527550/
https://www.ncbi.nlm.nih.gov/pubmed/31110237
http://dx.doi.org/10.1038/s41467-019-09691-z

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6527550/
https://www.ncbi.nlm.nih.gov/pubmed/31110237
http://dx.doi.org/10.1038/s41467-019-09691-z

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