Cargando…
The contribution of two isozymes to the pyruvate kinase activity of Vibrio cholerae: One K(+)-dependent constitutively active and another K(+)-independent with essential allosteric activation
In a previous phylogenetic study of the family of pyruvate kinase EC (2.7.1.40), a cluster with Glu117 and another with Lys117 were found (numbered according to the rabbit muscle enzyme). The sequences with Glu117 have been found to be K(+)-dependent, whereas those with Lys117 were K(+)-independent....
Autores principales: | Guerrero-Mendiola, Carlos, García-Trejo, José J., Encalada, Rusely, Saavedra, Emma, Ramírez-Silva, Leticia |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5501398/ https://www.ncbi.nlm.nih.gov/pubmed/28686591 http://dx.doi.org/10.1371/journal.pone.0178673 |
Ejemplares similares
-
Exploring the differences between the three pyruvate kinase isozymes from Vibrio cholerae in a heterologous expression system
por: Alba-Martínez, Zoe, et al.
Publicado: (2018) -
New Insights on the Mechanism of the K(+)-Independent Activity of Crenarchaeota Pyruvate Kinases
por: De la Vega-Ruíz, Gustavo, et al.
Publicado: (2015) -
Correction: New Insights on the Mechanism of the K(+)-Independent Activity of Crenarchaeota Pyruvate Kinases
por: De la Vega-Ruíz, Gustavo, et al.
Publicado: (2015) -
The Importance of Polarity in the Evolution of the K(+) Binding Site of Pyruvate Kinase
por: Ramírez-Silva, Leticia, et al.
Publicado: (2014) -
The K(+)-Dependent and -Independent Pyruvate Kinases Acquire the Active Conformation by Different Mechanisms
por: Ramírez-Silva, Leticia, et al.
Publicado: (2022)