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Results 1 - 10 of 10
EC Number Posttranslational Modification Commentary Reference
Show all pathways known for 4.2.1.3Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.3acetylation 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 747087
Show all pathways known for 4.2.1.3Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.3more a postranslational activation-inactivation mechanism might be operating 33814
Show all pathways known for 4.2.1.3Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.3more identification of two mitochondrial forms of enzyme with N-formylkynurenine modifications 681626
Show all pathways known for 4.2.1.3Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.3phosphoprotein 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 677458
Show all pathways known for 4.2.1.3Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.3phosphoprotein mechanism controlling IRP1 activity at the level of its stability can be phosphorylation of Ser138, Ser138, Ser711, and flanking sequences are highly conserved 696168
Show all pathways known for 4.2.1.3Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.3phosphoprotein phosphorylation of mitochondrial aconitase by PKCbeta2 has regulatory function, overview 697220
Show all pathways known for 4.2.1.3Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.3phosphoprotein S711 is a phosphorylation site 663958
Show all pathways known for 4.2.1.3Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.3phosphoprotein S711 of IRP1 is phosphorylated by proteinkinase C in vitro and in vivo in human HEK cells. Aconitase activity of the S711 phosphomimetic mutants is preferentially inhibited in the citrate mode of aconitase function. The substitution of phosphomimetic amino acids for S711 fails to affect the RNA-binding affinity of IRP1 666706
Show all pathways known for 4.2.1.3Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.3proteolytic modification the porcine heart enzyme is synthesized as a precursor containing a mitochondrial targeting sequence of 27 amino acid residues which is cleaved to yield a mature enzyme of 754 amino acids 33813
Show all pathways known for 4.2.1.3Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.3side-chain modification traces of carbohydrate of less than 1% 33789
Results 1 - 10 of 10