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Literature summary for 4.2.1.3 extracted from

  • Tortora, V.; Quijano, C.; Freeman, B.; Radi, R.; Castro, L.
    Mitochondrial aconitase reaction with nitric oxide, S-nitrosoglutathione, and peroxynitrite: mechanisms and relative contributions to aconitase inactivation (2007), Free Radic. Biol. Med., 42, 1075-1088.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Sus scrofa

Crystallization (Commentary)

Crystallization (Comment) Organism
computational modeling of aconitase inactivation by superoxide and nitric oxide Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
nitric oxide brief exposure leads to a reversible inhibition competitive with isocitrate. subsequently, an irreversible inactivation is observed Sus scrofa
nitrosoglutathione irreversible inactivation both in presence and absence of substrate Sus scrofa
peroxynitrite reacts with [4Fe-4S] cluster yielding an inactive [3Fe-4S] enzyme. Carbon dioxide enhances the reaction. Peroxynitrite also induces aconitase tyrosine nitration, without contributing to inactivation Sus scrofa

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Iron [4Fe-4S] cluster Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
Sus scrofa
-

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.035
-
nitric oxide reversible inhibition after brief exposure Sus scrofa