AI Article Synopsis
- The study investigated how the yeast Pichia guilliermondii synthesizes a riboflavin precursor called 6,7-dimethyl-8-ribityllumazine using rib5 and rib6 mutant strains.
- The rib5 mutant, which produces the active P1 protein, can synthesize the precursor when provided with specific substrates, while the rib6 mutant, which produces the inactive P2 protein, cannot.
- Results suggest that P1 and P2 proteins work together in this biosynthesis, with P1 facilitating the reaction and P2 required for utilizing ribose-5-phosphate as an intermediate.
Article Abstract
The biosynthesis of riboflavin precursor 6,7-dimethyl-8-ribityllumazine was studied in extracts of Pichia guilliermondii yeast mutants of rib5 and rib6 genotypes with impaired synthesis of proteins P1 and P2, respectively. It was shown that synthesis of 6,7-dimethyl-8-ribityllumazine took place in extracts of rib5 mutant (active P1 protein) in the presence of 2,4-dihydroxy-5-amino-6-ribitylaminopyrimidine and the compound formed from ribose-5-phosphate by extracts of rib6 mutant (active P2 protein). No lumazine was formed in extracts of rib6 mutant from pyrimidine substrate and ribose-5-phosphate preincubated with extracts of rib5 mutant. Hence, P1 protein (the product of RIB5 gene) participates in the biosynthesis of 6,7-dimethyl-8-ribityllumazine from 2,4-dihydroxy-5-amino-6-ribitylaminopyrimidine and aliphatic intermediate which is formed from ribose-5-phosphate, under the action of P2 protein (the product of RIB6 gene).
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