Cargando…
Kinetics and thermodynamics of the protein-ligand interactions in the riboflavin kinase activity of the FAD synthetase from Corynebacterium ammoniagenes
Enzymes known as bifunctional and bimodular prokaryotic type-I FAD synthetase (FADS) exhibit ATP:riboflavin kinase (RFK) and FMN:ATP adenylyltransferase (FMNAT) activities in their C-terminal and N-terminal modules, respectively, and produce flavin mononucleotide (FMN) and flavin adenine dinucleotid...
Autores principales: | Sebastián, María, Serrano, Ana, Velázquez-Campoy, Adrián, Medina, Milagros |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5544777/ https://www.ncbi.nlm.nih.gov/pubmed/28779158 http://dx.doi.org/10.1038/s41598-017-07875-5 |
Ejemplares similares
-
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) -
The trimer interface in the quaternary structure of the bifunctional prokaryotic FAD synthetase from Corynebacterium ammoniagenes
por: Serrano, Ana, et al.
Publicado: (2017) -
Specific Features for the Competent Binding of Substrates at the FMN Adenylyltransferase Site of FAD Synthase from Corynebacterium ammoniagenes
por: Arilla-Luna, Sonia, et al.
Publicado: (2019) -
The FAD synthetase from the human pathogen Streptococcus pneumoniae: a bifunctional enzyme exhibiting activity-dependent redox requirements
por: Sebastián, María, et al.
Publicado: (2017)