Mutations in sdh (succinate dehydrogenase genes) alter the thiamine requirement of Salmonella typhimurium

J Bacteriol. 1997 Jun;179(12):3989-96. doi: 10.1128/jb.179.12.3989-3996.1997.


Mutants lacking the first enzyme in de novo purine synthesis (PurF) can synthesize thiamine if increased levels of pantothenate are present in the culture medium (J. L. Enos-Berlage and D. M. Downs, J. Bacteriol. 178:1476-1479, 1996). Derivatives of purF mutants that no longer required pantothenate for thiamine-independent growth were isolated. Analysis of these mutants demonstrated that they were defective in succinate dehydrogenase (Sdh), an enzyme of the tricarboxylic acid cycle. Results of phenotypic analyses suggested that a defect in Sdh decreased the thiamine requirement of Salmonella typhimurium. This reduced requirement correlated with levels of succinyl-coenzyme A (succinyl-CoA), which is synthesized in a thiamine pyrophosphate-dependent reaction. The effect of succinyl-CoA on thiamine metabolism was distinct from the role of pantothenate in thiamine synthesis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acyl Coenzyme A / metabolism
  • Mutation
  • Pantothenic Acid / physiology
  • Salmonella typhimurium / metabolism*
  • Succinate Dehydrogenase / genetics
  • Succinate Dehydrogenase / physiology*
  • Succinates / pharmacology
  • Succinic Acid
  • Thiamine / biosynthesis*


  • Acyl Coenzyme A
  • Succinates
  • Pantothenic Acid
  • Succinic Acid
  • succinyl-coenzyme A
  • Succinate Dehydrogenase
  • Thiamine