Biosynthesis of the pyrimidine moiety of thiamine independent of the PurF enzyme (phosphoribosylpyrophosphate amidotransferase) in Salmonella typhimurium: incorporation of stable isotope-labeled glycine and formate

Research was conducted to examine the proposed synthesis that the pyrimidine moiety of thiamine can be characterized independently of the first enzyme of the de novo purine synthesis, phosphoribosylpyrophosphate amidotransferase (PurF), in Salmonella typhimurium. Isotope labeling experiments were carried out with two compounds, (2-(super 13)C)glycine and (super 13C)formate. Results demonstrate that PurF-independent TPP synthesis did not function at the same capacity as that involving the PurF enzyme.