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Literature summary for 1.8.1.4 extracted from

  • Yan, L.J.; Sumien, N.; Thangthaeng, N.; Forster, M.J.
    Reversible inactivation of dihydrolipoamide dehydrogenase by mitochondrial hydrogen peroxide (2013), Free Radic. Res., 47, 123-133.
    View publication on PubMedView publication on EuropePMC
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Inhibitors

Inhibitors Comment Organism Structure
H2O2 enzyme is inactivated by complex III- but not complex I-derived reactive oxygen species, and the accompanying loss of activity due to the inactivation can be restored by cysteine and glutathione. H2O2 instead of superoxide anion is responsible for the inactivation, and protein sulfenic acid formation is associated with the loss of enzymatic activity Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Rattus norvegicus 5739
-

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Rattus norvegicus
-

General Information

General Information Comment Organism
metabolism enzyme is inactivated by complex III- but not complex I-derived reactive oxygen species, and the accompanying loss of activity due to the inactivation can be restored by cysteine and glutathione. H2O2 instead of superoxide anion is responsible for the inactivation, and protein sulfenic acid formation is associated with the loss of enzymatic activity Rattus norvegicus