Disulfide-bond oxidoreductase YghU
UniProtKB accession: Q46845
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Go to UniProtKB: Q46845
UniProtKB description: Exhibits a robust glutathione (GSH)-dependent disulfide-bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Also displays a modest GSH-dependent peroxidase activity toward several organic hydroperoxides, such as cumene hydroperoxide and linoleic acid 13(S)-hydroperoxide, but does not reduce H(2)O(2) or tert-butyl hydroperoxide at appreciable rates. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) with glutathionylspermidine (GspSH) as the nucleophilic substrate.
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