Cargando…
Analysis of the Structure-Function-Dynamics Relationships of GALT Enzyme and of Its Pathogenic Mutant p.Q188R: A Molecular Dynamics Simulation Study in Different Experimental Conditions
The third step of the catabolism of galactose in mammals is catalyzed by the enzyme galactose-1-phosphate uridylyltransferase (GALT), a homodimeric enzyme with two active sites located in the proximity of the intersubunit interface. Mutations of this enzyme are associated to the rare inborn error of...
Autores principales: | Verdino, Anna, D’Urso, Gaetano, Tammone, Carmen, Scafuri, Bernardina, Marabotti, Anna |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8513031/ https://www.ncbi.nlm.nih.gov/pubmed/34641485 http://dx.doi.org/10.3390/molecules26195941 |
Ejemplares similares
-
Simulation of the Interactions of Arginine with Wild-Type GALT Enzyme and the Classic Galactosemia-Related Mutant p.Q188R by a Computational Approach
por: Verdino, Anna, et al.
Publicado: (2021) -
Arginine does not rescue p.Q188R mutation deleterious effect in classic galactosemia
por: Haskovic, Minela, et al.
Publicado: (2018) -
GALT Protein Database, a Bioinformatics Resource for the Management and Analysis of Structural Features of a Galactosemia-related Protein and Its Mutants
por: d’Acierno, Antonio, et al.
Publicado: (2009) -
Performance of Web tools for predicting changes in protein stability caused by mutations
por: Marabotti, Anna, et al.
Publicado: (2021) -
D'Amour, P.Q.; roman /
por: Godbout, Jacques, 1933-
Publicado: (1972)