Literature summary 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.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
4.2.1.3	expression in Escherichia coli	Sus scrofa

Crystallization (Commentary)

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

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
4.2.1.3	nitric oxide	brief exposure leads to a reversible inhibition competitive with isocitrate. subsequently, an irreversible inactivation is observed	Sus scrofa
4.2.1.3	nitrosoglutathione	irreversible inactivation both in presence and absence of substrate	Sus scrofa
4.2.1.3	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

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

Metals/Ions

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

Organism

EC Number	Organism	UniProt	Comment	Textmining
4.2.1.3	Sus scrofa	-	-	-

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
4.2.1.3	heart	-	Sus scrofa	-

Ki Value [mM]

EC Number	Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
4.2.1.3	0.035	-	nitric oxide	reversible inhibition after brief exposure	Sus scrofa

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Release 2023.1 (January 2023)