Article
Repurposing lipoic acid changes electron flow in two important metabolic pathways of Escherichia coli.
Proceedings of the National Academy of Sciences of the United States of America - 10 May 2011
Feeney Morgan Anne, Veeravalli Karthik, Boyd Dana, Gon Stéphanie, Faulkner Melinda Jo, Georgiou George, Beckwith Jonathan
Abstract excerpt
In bacteria, cysteines of cytoplasmic proteins, including the essential enzyme ribonucleotide reductase (RNR), are maintained in the reduced state by the thioredoxin and glutathione/glutaredoxin pathways. An Escherichia coli mutant lacking both glutathione reductase and thioredoxin reductase cannot grow because RNR is disulfide bonded and nonfunctional. Here we report that suppressor mutations in the lpdA gene,...
Topics
- Base Sequence
- Citric Acid Cycle
- Cytoplasm
- DNA Primers
- DNA, Bacterial
- Dihydrolipoamide Dehydrogenase
- Electron Transport
- Escherichia coli
- Escherichia coli Proteins
- Genes, Bacterial
- Glutaredoxins
- Glutathione Reductase
