The Escherichia coli btuE gene, encodes a glutathione peroxidase that is induced under oxidative stress conditions.

ABSTRACT: Most aerobic organisms are exposed to oxidative stress. Looking for enzyme activities involved in the bacterial response to this kind of stress, we focused on the btuE-encoded Escherichia coli BtuE, an enzyme that shares homology with the glutathione peroxidase (GPX) family. This work deals with the purification and characterization of the btuE gene product. Purified BtuE decomposes in vitro hydrogen peroxide in a glutathione-dependent manner. BtuE also utilizes preferentially thioredoxin A to decompose hydrogen peroxide as well as cumene-, tert-butyl-, and linoleic acid hydroperoxides, confirming that its active site confers non-specific peroxidase activity. These data suggest that the enzyme may have one or more organic hydroperoxide as its physiological substrate. The btuE gene was indu

SUBMITTER: Arenas FA 

PROVIDER: S-EPMC3057470 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature