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Literature summary for 1.1.1.42 extracted from

  • Kil, I.S.; Park, J.W.
    Regulation of mitochondrial NADP+-dependent isocitrate dehydrogenase activity by glutathionylation (2005), J. Biol. Chem., 280, 10846-10854.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
glutathione oxidized glutathione leads to enzyme inactivation with simultaneous formation of a mixed disulfide between glutathione and the cysteine residues of enzyme. Enzymical reactivation by glutaredoxin2 in presence of reduced glutathione Sus scrofa

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Sus scrofa 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Sus scrofa during oxidative stress, enzyme activity appears to be modulated through enzymatic glutathionylation and deglutathionylation ?
-
?

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
oxidized glutathione leads to enzyme inactivation with simultaneous formation of a mixed disulfide between glutathione and the cysteine residues of enzyme. Enzymical reactivation by glutaredoxin2 in presence of reduced glutathione Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information during oxidative stress, enzyme activity appears to be modulated through enzymatic glutathionylation and deglutathionylation Sus scrofa ?
-
?