DECR1 Human

DECR1 is an auxiliary enzyme involved in the beta-oxidation pathway, specifically targeting unsaturated fatty enoyl-CoA esters with double bonds in both even- and odd-numbered positions . It catalyzes the NADPH-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA . This reaction is essential for the degradation of polyunsaturated fatty acids, which require additional enzymatic steps compared to saturated fatty acids .

The enzyme exists as a homotetramer in physiological conditions but can also form monomers and dimers in solution . It belongs to the short-chain dehydrogenase/reductase (SDR) superfamily and shares many structural motifs with other SDR enzymes, including a Rossmann fold for strong NADPH binding . Key residues in the enzyme’s active site facilitate the hydride transfer through a network of hydrogen bonds .

DECR1 is present in both the mitochondria (mDECR) and the peroxisome (pDECR), with each organelle’s enzyme being homologous . The mitochondrial form is involved in the beta-oxidation of fatty acids, while the peroxisomal form handles very long-chain fatty acids before they are further processed in the mitochondria .

Recombinant DECR1 is used in various research applications to study its role in fatty acid metabolism and its potential implications in metabolic disorders. Understanding the enzyme’s function and structure can provide insights into developing therapeutic strategies for conditions related to fatty acid metabolism.