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

Ítems similars

• Synthesis of thiamine in Salmonella typhimurium independent of the purF function.
  per: Downs, D M, et al.
  Publicat: (1991)
• Amino-terminal deletions define a glutamine amide transfer domain in glutamine phosphoribosylpyrophosphate amidotransferase and other PurF-type amidotransferases.
  per: Mei, B G, et al.
  Publicat: (1990)
• Evidence for a new, oxygen-regulated biosynthetic pathway for the pyrimidine moiety of thiamine in Salmonella typhimurium.
  per: Downs, D M
  Publicat: (1992)
• Involvement of the oxidative pentose phosphate pathway in thiamine biosynthesis in Salmonella typhimurium.
  per: Enos-Berlage, J L, et al.
  Publicat: (1996)
• Mutations in the Tryptophan Operon Allow PurF-Independent Thiamine Synthesis by Altering Flux In Vivo
  per: Ramos, Itzel, et al.
  Publicat: (2008)