Reference - Detail
| RRC ID | 4934 |
|---|---|
| Author | Tao K. |
| Title | Subcellular localization and in vivo oxidation-reduction kinetics of thiol peroxidase in Escherichia coli. |
| Journal | FEMS Microbiol Lett |
| Abstract |
Peroxiredoxins are a class of peroxide-scavenging enzymes having a conserved cysteine residue(s) in their active centers. Thiol peroxidase (Tpx) is one of the peroxiredoxins identified in Escherichia coli. Despite the absence of the N-terminal signal sequence for transport across the membrane, it has been characterized as a periplasmic protein. Reanalysis of Tpx localization, using active site cysteine mutants of thioredoxin 1 (Trx1), demonstrated that Tpx forms a mixed-disulfide complex with cytoplasmic Trx1, indicating that Tpx localizes in the cytoplasm. |
| Volume | 289(1) |
| Pages | 41-5 |
| Published | 2008-12-1 |
| DOI | 10.1111/j.1574-6968.2008.01372.x |
| PII | FML1372 |
| PMID | 19054092 |
| MeSH | Cell Fractionation / methods* Cytoplasm / enzymology* Escherichia coli K12 / enzymology* Escherichia coli K12 / genetics Escherichia coli Proteins / genetics Escherichia coli Proteins / metabolism* Hydrogen Peroxide Kinetics Mutation Osmotic Pressure Oxidation-Reduction Periplasmic Proteins / genetics Periplasmic Proteins / metabolism* Peroxidases / genetics Peroxidases / metabolism* Plasmids / genetics Spheroplasts Thioredoxins / genetics Thioredoxins / metabolism |
| IF | 1.987 |
| Times Cited | 12 |
| WOS Category | MICROBIOLOGY |
| Resource | |
| Prokaryotes E. coli | Keio collection ME9062(JM109(DE3)) ASKA(JW1317) |