RRC ID 4934
著者 Tao K.
タイトル Subcellular localization and in vivo oxidation-reduction kinetics of thiol peroxidase in Escherichia coli.
ジャーナル 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.
巻・号 289(1)
ページ 41-5
公開日 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
引用数 12
WOS 分野 MICROBIOLOGY
リソース情報
原核生物(大腸菌) Keio collection ME9062(JM109(DE3)) ASKA(JW1317)