The FAD synthetase from the human pathogen Streptococcus pneumoniae: a bifunctional enzyme exhibiting activity-dependent redox requirements. [electronic resource]
Producer: 20190219Description: 7609 p. digitalISSN:- 2045-2322
- 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
No physical items for this record
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
There are no comments on this title.
Log in to your account to post a comment.