EC Number |
Title |
Organism |
---|
2.5.1.9 | A high-throughput screening for inhibitors of riboflavin synthase identifies novel antimicrobial compounds to treat brucellosis |
Brucella abortus |
2.5.1.9 | The C-terminal peptide of Aquifex aeolicus riboflavin synthase directs encapsulation of native and foreign guests by a cage-forming lumazine synthase |
Aquifex aeolicus |
2.5.1.9 | The roseoflavin producer Streptomyces davaonensis has a high catalytic capacity and specific genetic adaptations with regard to the biosynthesis of riboflavin |
Streptomyces davaonensis |
2.5.1.9 | 4-(1'-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine, the second product of the riboflavin synthetase reaction |
Saccharomyces cerevisiae |
2.5.1.9 | A new series of N-[2,4-dioxo-6-d-ribitylamino-1,2,3,4-tetrahydropyrimidin-5-yl]oxalamic acid derivatives as inhibitors of lumazine synthase and riboflavin synthase: design, synthesis, biochemical evaluation, crystallography, and mechanistic implications |
Escherichia coli |
2.5.1.9 | Assay methods, isolation procedures, and catalytic properties of riboflavin synthetase from spinach |
Saccharomyces cerevisiae |
2.5.1.9 | Assay methods, isolation procedures, and catalytic properties of riboflavin synthetase from spinach |
Spinacia oleracea |
2.5.1.9 | Biosynthesis of riboflavin. 6,7-Dimethyl-8-ribityllumazine 5-phosphate is not a substrate for riboflavin synthase |
Bacillus subtilis |
2.5.1.9 | Biosynthesis of riboflavin. 6,7-Dimethyl-8-ribityllumazine 5-phosphate is not a substrate for riboflavin synthase |
Escherichia coli |
2.5.1.9 | Biosynthesis of riboflavin. Enzymatic formation of 6,7-dimethyl-8-ribityllumazine by heavy riboflavin synthase from Bacillus subtilis |
Bacillus subtilis |