The PECR gene encodes a protein that consists of 303 amino acids and has a molecular mass of approximately 33 kDa . The protein contains a C-terminal type I peroxisomal targeting signal (AKL), which is essential for its localization to the peroxisome . The enzyme is a member of the short-chain dehydrogenase/reductase (SDR) family and is highly conserved across species, sharing 71-75% amino acid identity with its homologs in guinea pig and mouse .
PECR is involved in the chain elongation of fatty acids within the peroxisome . It catalyzes the reduction of trans-2-enoyl-CoAs of varying chain lengths, with maximum activity observed with 10:1 CoA . This reduction step is NADPH-specific, meaning that the enzyme uses NADPH as a cofactor to carry out the reduction reaction . The enzyme does not exhibit 2,4-dienoyl-CoA reductase activity .
The activity of PECR is essential for the proper functioning of the peroxisomal fatty acid β-oxidation pathway, which is crucial for the metabolism of very-long-chain fatty acids (VLCFAs) . Disruptions in this pathway can lead to the accumulation of VLCFAs, which are associated with various metabolic disorders .
Recombinant human PECR is used in research to study its enzymatic properties and to develop potential therapeutic interventions . The recombinant form of the enzyme is produced by expressing the PECR gene in suitable host cells, followed by purification of the protein . This allows researchers to investigate the enzyme’s structure, function, and role in various metabolic pathways.