Cargando…
The FAD synthetase from the human pathogen Streptococcus pneumoniae: a bifunctional enzyme exhibiting activity-dependent redox requirements
Prokaryotic bifunctional FAD synthetases (FADSs) catalyze the biosynthesis of FMN and FAD, whereas in eukaryotes two enzymes are required for the same purpose. FMN and FAD are key cofactors to maintain the flavoproteome homeostasis in all type of organisms. Here we shed light to the properties of th...
Autores principales: | Sebastián, María, Lira-Navarrete, Erandi, Serrano, Ana, Marcuello, Carlos, Velázquez-Campoy, Adrián, Lostao, Anabel, Hurtado-Guerrero, Ramón, Medina, Milagros, Martínez-Júlvez, Marta |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5548840/ https://www.ncbi.nlm.nih.gov/pubmed/28790457 http://dx.doi.org/10.1038/s41598-017-07716-5 |
Ejemplares similares
-
The trimer interface in the quaternary structure of the bifunctional prokaryotic FAD synthetase from Corynebacterium ammoniagenes
por: Serrano, Ana, et al.
Publicado: (2017) -
Role of Key Residues at the Flavin Mononucleotide (FMN):Adenylyltransferase Catalytic Site of the Bifunctional Riboflavin Kinase/Flavin Adenine Dinucleotide (FAD) Synthetase from Corynebacterium ammoniagenes
por: Serrano, Ana, et al.
Publicado: (2012) -
Structural analysis of FAD synthetase from Corynebacterium ammoniagenes
por: Frago, Susana, et al.
Publicado: (2008) -
Kinetics and thermodynamics of the protein-ligand interactions in the riboflavin kinase activity of the FAD synthetase from Corynebacterium ammoniagenes
por: Sebastián, María, et al.
Publicado: (2017) -
Nanomechanical Study of Enzyme: Coenzyme Complexes: Bipartite Sites in Plastidic Ferredoxin-NADP(+) Reductase for the Interaction with NADP(+)
por: Pérez-Domínguez, Sandra, et al.
Publicado: (2022)