Abstract
Riboflavin after conversion to flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) serves as an essential cofactor for mainstream metabolic enzymes which mediate hydride, oxygen, and electron transfer catalytic functions (1). Enzymes of the riboflavin biosynthetic pathway are attractive targets for the rational design of antibiotics and crop protection chemicals since humans do not synthesize riboflavin (also known as vitamin B2) and must obtain it through their diets (2). Indeed, there are design and synthesis reports regarding the penultimate and ultimate enzymes of the biosynthetic pathway, 6,7-dimethyl-8-(1’D-ribityl)-lumazine synthase (lumazine synthase) and riboflavin synthase, respectively (3–5).
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