Ontology highlight
ABSTRACT:
SUBMITTER: Sevier CS
PROVIDER: S-EPMC2253379 | biostudies-literature | 2005 Jun
REPOSITORIES: biostudies-literature
Sevier Carolyn S CS Kadokura Hiroshi H Tam Vincent C VC Beckwith Jon J Fass Deborah D Kaiser Chris A CA
Protein science : a publication of the Protein Society 20050601 6
Three different classes of thiol-oxidoreductases that facilitate the formation of protein disulfide bonds have been identified. They are the Ero1 and SOX/ALR family members in eukaryotic cells, and the DsbB family members in prokaryotic cells. These enzymes transfer oxidizing potential to the proteins PDI or DsbA, which are responsible for directly introducing disulfide bonds into substrate proteins during oxidative protein folding in eukaryotes and prokaryotes, respectively. A comparison of the ...[more]