DECR2 Human

2,4-Dienoyl CoA Reductase 2 (DECR2) is an enzyme that plays a crucial role in the beta-oxidation pathway of polyunsaturated fatty acids. This enzyme is encoded by the DECR2 gene located on chromosome 16p13.3 . DECR2 is primarily found in the peroxisomes of cells and is involved in the degradation of unsaturated fatty enoyl-CoA esters that have double bonds in both even- and odd-numbered positions .

The human recombinant form of 2,4-Dienoyl CoA Reductase 2 is typically produced in Escherichia coli (E. coli) expression systems. The recombinant protein is a single, non-glycosylated polypeptide chain containing 315 amino acids and has a molecular mass of approximately 33.2 kDa . The protein is fused to a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques . The final product is a sterile filtered colorless solution, formulated with 20mM Tris-HCl buffer (pH 8.0), 40% glycerol, 0.15M NaCl, and 1mM DTT .

2,4-Dienoyl CoA Reductase 2 catalyzes the NADPH-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA . This reaction is a critical step in the beta-oxidation of polyunsaturated fatty acids, allowing the fatty acid to be further processed by the standard beta-oxidation pathway . The enzyme is capable of reducing both 2-trans,4-cis-dienoyl-CoA and 2-trans,4-trans-dienoyl-CoA thioesters with equal efficiency . This lack of stereospecificity is unusual for enzymes, which are typically highly stereoselective .

The enzyme’s active site contains key residues that orient the substrate for hydride transfer through a network of hydrogen bonds . The enolate intermediate formed during the reaction is stabilized by additional hydrogen bonds to specific residues such as Tyr166 and Asn148 . The enzyme also has a flexible loop at one end of the active site, providing sufficient room for long carbon chains, which likely gives the enzyme the flexibility to process fatty acid chains of various lengths .