Literature summary for 4.2.1.3 extracted from

Zhang, S.; Sandstroem, M.E.; Lanner, J.T.; Thorell, A.; Westerblad, H.; Katz, A.
Activation of aconitase in mouse fast-twitch skeletal muscle during contraction-mediated oxidative stress (2007), Am. J. Physiol., 293, C1154-C1159.

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Inhibitors

Inhibitors	Comment	Organism	Structure
hydrogen peroxide	inhibits enzyme activity in cell-free extracts	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-
Mus musculus	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	aconitase is phosphorylated on serine residues. Increase in extensor digitorum longus muscle enzyme activity upon repeated contraction is inhibited by cyclosporin A, an inhibitor of the protein phosphates calcineurin	Mus musculus

Source Tissue

Source Tissue	Comment	Organism	Textmining
extensor digitorum longus	repeated contractions increase aconitase activity by 50%. Increase is not accompanied by increase in aconitase protein, but is markedly inhibited by cyclosporin A	Mus musculus	-
skeletal muscle	muscle exercise does not affect aconitase activity despite increased oxidative stress	Homo sapiens	-
soleus	repeated contractionsdo not alter aconitase activity	Mus musculus	-

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Release 2023.1 (January 2023)