PMID: 9190816Jun 1, 1997Paper

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

Journal of Bacteriology
J Enos-Berlage, D M Downs

Abstract

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.

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Citations

Dec 8, 2010·Genetics·Jannell V Bazurto, Diana M Downs
Jun 15, 2006·Annual Review of Microbiology·Diana M Downs
Dec 4, 2013·Journal of Bacteriology·Jannell V Bazurto, Diana M Downs
May 29, 2001·The Journal of Biological Chemistry·A R HorswillJ C Escalante-Semerena
Jan 21, 2003·Journal of Bacteriology·Glenn R Björk, Kristina Nilsson
Dec 28, 1999·Methods : a Companion to Methods in Enzymology·D M Downs, J C Escalante-Semerena
Apr 1, 2007·EcoSal Plus·Roberta Leonardi, Suzanne Jackowski

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