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IDI1, through its highly electrophilic isomers, encodes a peroxide localization enzyme that catalyzes the interconversion of isoprene (IPP) and dimethyl diphosphate (DMAPP). Dimethyl diphosphate (DMAPP) is a substrate for the continuous reaction and is eventually used to synthesize cholesterol. Peroxidase defects such as zierweg syndrome and neonatal adrenal leukodystrophy, IPP isomerase activity is decreased.
Figure 1. The mechanism for the isomerization between IDI and DMAPP.
Isoprene isomerase (IDI) activates isoprene (IPP) polymerization by converting isoprene (IPP) into its highly nucleophilic dimethylallyl diphosphate (DMAPP). In plants, the central reaction of isoprene biosynthesis is catalyzed by highly conserved isoenzymes with different expression patterns and subcellular localization. Unlike plants, only IDI1 is highly conserved in mammals and is most likely responsible for housekeeping isomerase activity. The second isomer, IDI2, is more diffuse. We demonstrate that the active center changes during the initial repeat IDI2 after a short period of significant random change. Since then, IDI2 has been under strict purification options for at least 70 million years. The molecular model indicated that the modified IDI2 could still catalyze IPP isomerization to DMAPP. In humans, IDI2 is expressed only at high levels in skeletal muscles, where it may be involved in the specific production of isoprene for post-translational modifications of proteins. IDI2, revealed by sequence conservative patterns, has significant positive fitness effects, and its specific expression patterns emphasize the importance of IDI gene replication in mammals.
While there have been no evidence directly implicating IDI1 mutations in human disease, genomic analysis has identified a copy-number gain near two IDI isomerase genes in a substantial proportion of patients with sporadic amyotrophic lateral sclerosis, suggesting that the isomerase may play a role in this disease. IDI is a cytoplasmic enzyme involved in the biosynthesis of isoprene including cholesterol. Scientists studied immunohistochemical localization of Eddie 1 and Eddie 2 in patients with PLB and multiple system atrophy (MSA). In the normal control group, the neuronal cytoplasm was weakly immunostained with anti-IDI1 and anti-IDI2 antibodies throughout the nervous system. In LB disease, brain-derived LBs had a strong positive response to IDI1 and IDI2, and cortex LBs had no or little immunological markers. Double immunofluorescence staining revealed the phosphorylation of IDI1 or IDI2 of co-localization. Glial cytoplasmic inclusions in MSA were not stained. Previous studies have shown that cholesterol metabolites increase the number of pounds of disease, and in the cerebral cortex of patients, these metabolites accelerate the aggregation of synuclein. Current results suggest that IDI1 and IDI2 may be related to the production of cholesterol metabolites, leading to the formation of pounds during the polymerization of selective synuclein.