IDI2 Human
Isopentenyl-diphosphate Delta-isomerase 2, Isopentenyl pyrophosphate isomerase 2, IPP isomerase 2, IPPI2, IDI2.
Description
IDI2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 247 amino acids (1-227 a.a.) and having a molecular mass of 28.9kDa.
IDI2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
The enzyme Isopentenyl-diphosphate Delta-isomerase 2, often shortened to IDI2, belongs to the IPP isomerase type 1 family. IDI2 facilitates the conversion of isopentenyl (IPP) into dimethylallyl diphosphate (DMAPP) through a 1,3-allylic rearrangement. This transformation is crucial as DMAPP is a highly reactive electrophilic molecule.
Produced in E.Coli, our IDI2 is a single, non-glycosylated polypeptide chain. It comprises 247 amino acids (specifically, amino acids 1 to 227) and has a molecular weight of 28.9kDa. For purification and ease of use, a 20 amino acid His-tag is fused to the N-terminus of IDI2. The protein is then purified using proprietary chromatographic methods.
Isopentenyl-diphosphate Delta-isomerase 2, Isopentenyl pyrophosphate isomerase 2, IPP isomerase 2, IPPI2, IDI2.
Product Science Overview
The IDI2 gene is a protein-coding gene located on chromosome 10 in humans. It is a product of an ancestral gene duplication event and has a paralog known as IDI1 . The protein encoded by this gene is involved in the aggregation of alpha-synuclein in the cerebral cortex of patients with Lewy body disease and has been associated with sporadic amyotrophic lateral sclerosis .
IDI2 catalyzes the isomerization of IPP to DMAPP through a 1,3-allylic rearrangement. This reaction involves the antarafacial transposition of hydrogen, proceeding by a protonation/deprotonation mechanism. The addition of a proton to the re-face of the inactivated C3-C4 double bond results in a transient carbocation intermediate, followed by the removal of the pro-R proton from C2 to form the C2-C3 double bond of DMAPP .
Crystallographic studies have shown that the active form of IDI2 is a monomer with alternating α-helices and β-sheets. The active site of the enzyme is deeply buried within the protein and consists of a glutamic acid residue and a cysteine residue that interact with opposite sides of the IPP substrate . This structure is consistent with the antarafacial stereochemistry of the isomerization reaction.
IDI2 is involved in the biosynthesis of cholesterol and other isoprenoids, which are vital for various cellular functions. The enzyme’s activity is crucial for maintaining the balance of these compounds in the body. Additionally, segmental copy number gains in the IDI2 locus have been linked to certain neurological disorders, highlighting its importance in human health .
Human recombinant IDI2 is used in research to study its role in isoprenoid biosynthesis and its involvement in diseases such as Lewy body disease and amyotrophic lateral sclerosis. Understanding the enzyme’s function and mechanism can lead to the development of therapeutic strategies for these conditions.
