Finally, aconitase is thought to be associated with diabetes . ) and genetic diabetes, lower aconitase activity was found to decrease the rates of metabolic reactions involving citrate, pyruvate, and malate.
22.
For example, in the presence of low iron concentrations, aconitase functions as an enzyme while at high iron concentration, aconitase functions as an iron-responsive element-binding protein ( IREBP ).
23.
For example, in the presence of low iron concentrations, aconitase functions as an enzyme while at high iron concentration, aconitase functions as an iron-responsive element-binding protein ( IREBP ).
24.
Mutant IRE-BPs, in which any or all of the three Cys residues involved in Fe-S formation are replaced by serine, have no aconitase activity, but retain RNA-binding properties.
25.
These include oxidation of iron-containing proteins such as ribonucleotide reductase and aconitase, activation of the soluble guanylate cyclase, ADP ribosylation of proteins, protein sulfhydryl group nitrosylation, and iron regulatory factor activation.
26.
A proposed mechanism for this connection is that decreased Fe-S activity in aconitase and succinate dehydrogenase is correlated with excess iron concentration in the mitochondria and insufficient iron in the cytoplasm, disrupting iron homeostasis.
27.
When this happens, the aconitase is converted to IRPF1, a translation repressor or mRNA stabilizer that represses the formation of iron-binding proteins and favours formation of proteins that can get iron from the cell's reservations
28.
The most sensitive targets of NO are aconitase, an enzyme that catalyzes the isomerization of citrate to isocitrate in the citric acid cycle, and cytochrome oxidase, the last enzyme in the respiratory electron transport chain of mitochondria.
29.
The iron-responsive element-binding protein ( IRE-BP ) and 3-isopropylmalate dehydratase ( ?-isopropylmalate isomerase; ), an enzyme catalysing the second step in the biosynthesis of leucine, are known aconitase homologues.
30.
Expression of IRE-BP in cultured cells has revealed that the protein functions either as an active aconitase, when cells are iron-replete, or as an active RNA-binding protein, when cells are iron-depleted.
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