The FAD synthetase from the human pathogen Streptococcus pneumoniae: a bifunctional enzyme exhibiting activity-dependent redox requirements. [electronic resource]
- Scientific reports 08 2017
- 7609 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
2045-2322
10.1038/s41598-017-07716-5 doi
Bacterial Proteins--antagonists & inhibitors Binding Sites Cloning, Molecular Dithionite--pharmacology Enzyme Inhibitors--pharmacology Escherichia coli--genetics Flavin Mononucleotide--biosynthesis Flavin-Adenine Dinucleotide--biosynthesis Gene Expression Kinetics Magnesium Chloride--pharmacology Models, Molecular Nucleotidyltransferases--antagonists & inhibitors Oxidation-Reduction Phosphotransferases (Alcohol Group Acceptor)--antagonists & inhibitors Protein Binding Protein Conformation, alpha-Helical Protein Conformation, beta-Strand Protein Interaction Domains and Motifs Protein Multimerization Recombinant Proteins--chemistry Riboflavin--chemistry Streptococcus pneumoniae--drug effects Substrate Specificity