Literature summary for 4.2.1.3 extracted from

Fernandes, J.; Weddle, A.; Kinter, C.S.; Humphries, K.M.; Mather, T.; Szweda, L.I.; Kinter, M.
Lysine acetylation activates mitochondrial aconitase in the heart (2015), Biochemistry, 54, 4008-4018 .

Search for more literature for 4.2.1.3

Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	acetyl-CoA-driven acetylation leads to about 45% activation. The increase in activity is a result of increased maximal velocity	Mus musculus

Application

Application	Comment	Organism
medicine	a high fat diet (60% kcal from fat) shows significantly increased mitochondrial aconitase activity without changes in protein level and produces increased aconitase acetylation at multiple sites	Mus musculus

Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular modeling suggests acetylation at K144 may perturb the tertiary structure of the enzyme	Mus musculus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Mus musculus	5739	-

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q99KI0	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
acetylation	in vitro chemical acetylation with either acetic anhydride or acetyl-CoA results in increased aconitase activity that is reversed with SIRT3 treatment. Lysine residues K31, K138, K144, K401, K549, K689, K700, K701, and K723 represent the most responsive sites. A high fat diet (60% kcal from fat) also shows significantly increased mitochondrial aconitase activity without changes in protein level and produces increased aconitase acetylation at multiple sites	Mus musculus

Source Tissue

Source Tissue	Comment	Organism	Textmining
heart	-	Mus musculus	-

Synonyms

Synonyms	Comment	Organism
Aco2	-	Mus musculus

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Release 2023.1 (January 2023)