1. Fachbereich Biologie, Universität Konstanz, D-7750 Konstanz, F.G.R.;2. Institut für Mikrobiologie, Universität Hohenheim, D-7000 Stuttgart 70 G.F.R.
Abstract:
Phosphotransferase from carrot is shown to catalyze the phosphorylation of 6,7-dimethyl-8-ribityllumazine specifically at position 5′ of the ribityl side chain. The lumazine 5′-phosphate is neither a substrate nor an inhibitor of riboflavin synthase from Bacillus subtilis and Escherichia coli. It follows that the obligatory product of riboflavin synthase is riboflavin and not FMN.