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. [electronic resource]
- Journal of bacteriology Feb 1999
- 841-8 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
0021-9193
10.1128/JB.181.3.841-848.1999 doi
Amidophosphoribosyltransferase--biosynthesis Carbon Isotopes Chromatography, High Pressure Liquid Formates--metabolism Gas Chromatography-Mass Spectrometry Glycine--metabolism Salmonella typhimurium--enzymology Thiamine Monophosphate--metabolism Thiamine Pyrophosphate--biosynthesis