| Literature DB >> 416855 |
G Harzer, H Rokos, M K Otto, A Bacher, S Ghisla.
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.Entities:
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Year: 1978 PMID： 416855 DOI： 10.1016/0304-4165(78)90433-6
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002