Mutations in sdh (succinate dehydrogenase genes) alter the thiamine requirement of Salmonella typhimurium
| Autor: | Jodi L. Enos-Berlage, Diana M. Downs |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Salmonella typhimurium
Mutant Succinic Acid medicine.disease_cause Microbiology Pantothenic Acid Pantothenic acid medicine Thiamine Molecular Biology chemistry.chemical_classification Mutation biology Succinate dehydrogenase food and beverages Succinates Succinate Dehydrogenase Citric acid cycle De novo synthesis Enzyme Biochemistry chemistry biology.protein bacteria Acyl Coenzyme A human activities Research Article |
| Zdroj: | Journal of Bacteriology. 179:3989-3996 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.179.12.3989-3996.1997 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|