Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.2.1.3 extracted from

  • Bulteau, A.L.; Ikeda-Saito, M.; Szweda, L.I.
    Redox-dependent modulation of aconitase activity in intact mitochondria (2003), Biochemistry, 42, 14846-14855.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
H2O2 H2O2 does not exert its inhibitory effects by acting directly on the enzyme, rather inactivation appears to result from interactions between aconitase and a mitochondrial membrane component responsive to H2O2. Prolonged exposure of mitochondria to steady-state levels of H2O2 or O2- results in disassembly of the [4Fe-4S]2+ cluster, carbonylation, and protein degradation Rattus norvegicus

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Iron the enzyme contains a [4Fe-4S]2+ cluster Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-
Rattus norvegicus Sprague-Dawley
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
Rattus norvegicus
-