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ABSTRACT:
SUBMITTER: Mizrachi D
PROVIDER: S-EPMC5562517 | biostudies-literature | 2017 Sep
REPOSITORIES: biostudies-literature
Mizrachi Dario D Robinson Michael-Paul MP Ren Guoping G Ke Na N Berkmen Mehmet M DeLisa Matthew P MP
Nature chemical biology 20170619 9
Escherichia coli DsbB is a transmembrane enzyme that catalyzes the reoxidation of the periplasmic oxidase DsbA by ubiquinone. Here, we sought to convert membrane-bound DsbB into a water-soluble biocatalyst by leveraging a previously described method for in vivo solubilization of integral membrane proteins (IMPs). When solubilized DsbB variants were coexpressed with an export-defective copy of DsbA in the cytoplasm of wild-type E. coli cells, artificial oxidation pathways were created that effici ...[more]