PECI Human
Description
Biological Functions
PECI facilitates the isomerization of unsaturated fatty acid derivatives during β-oxidation:
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Substrate Specificity: Converts 3-cis-octenoyl-CoA to 2-trans-octenoyl-CoA with a specific activity of 27 units/mg .
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Catalytic Preference: Higher activity toward 3-trans enoyl-CoA substrates compared to 3-cis isomers .
Key Metabolic Pathways
| Pathway | Role of PECI |
|---|---|
| Peroxisomal β-oxidation | Isomerizes Δ³,Δ²-enoyl-CoA to Δ²,Δ¹-enoyl-CoA for subsequent hydration . |
| Bile acid synthesis | Supports side-chain shortening of cholesterol intermediates . |
Research Findings
Tissue Expression
Northern blot analysis confirms ubiquitous PECI mRNA expression, with elevated levels in:
Disease Associations
Experimental Models
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Knockout Studies: Impaired peroxisomal β-oxidation in murine models .
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Inhibitor Screens: Small-molecule inhibitors reduce cancer cell proliferation .
Clinical Relevance
Diagnostic Tools
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Antibody Applications: Rabbit polyclonal anti-PECI/ECI2 (ab224441) validated for:
Therapeutic Potential
Product Specs
MGSSHHHHHH SSGLVPRGSH MNRTAMRASQ KDFENSMNQV KLLKKDPGNE VKLKLYALYK QATEGPCNMP KPGVFDLINK AKWDAWNALG SLPKEAARQN YVDLVSSLSP SLESSSQVEP GTDRKSTGFE TLVVTSEDGI TKIMFNRPKK KNAINTEMYH EIMRALKAAS KDDSIITVLT GNGDYYSSGN DLTNFTDIPP GGVEEKAKNN AVLLREFVGC FIDFPKPLIA VVNGPAVGIS VTLLGLFDAV YASDRATFHT PFSHLGQSPE GCSSYTFPKI MSPAKATEML IFGKKLTAGE ACAQGLVTEV FPDSTFQKEV WTRLKAFAKL PPNALRISKE VIRKREREKL HAVNAEECNV LQGRWLSDEC TNAVVNFLSR KSKL.
Product Science Overview
The enzyme plays a significant role in the beta-oxidation of unsaturated fatty acids, which is a key metabolic pathway for energy production in cells. Beta-oxidation occurs in both mitochondria and peroxisomes, with the peroxisomal pathway being particularly important for the breakdown of very long-chain fatty acids . The isomerase ensures that the double bonds in the fatty acid chains are correctly positioned for subsequent enzymatic reactions, facilitating efficient energy extraction from these molecules .
The isomerization reaction catalyzed by Peroxisomal D3,D2-Enoyl-CoA Isomerase involves the conversion of a 3-cis or 3-trans double bond to a 2-trans double bond. This reaction is crucial because the enzymes involved in the subsequent steps of beta-oxidation specifically recognize and act on 2-trans-enoyl-CoA . The mechanism involves the deprotonation of the C2 atom of the substrate by a catalytic residue, followed by the stabilization of the resulting conjugate base by an oxyanion hole formed by amide groups .
Structurally, Peroxisomal D3,D2-Enoyl-CoA Isomerase belongs to the crotonase superfamily and typically forms trimeric assemblies. The active site of the enzyme contains key residues that facilitate the isomerization reaction. For example, Glu158 acts as both a proton acceptor and donor during the reaction, while other residues like Ala70 and Leu126 stabilize the substrate’s conjugate base .
The human recombinant form of this enzyme is produced using recombinant DNA technology, which involves inserting the gene encoding the enzyme into a suitable expression system, such as bacteria or yeast. This allows for the production of large quantities of the enzyme for research and therapeutic purposes. The recombinant enzyme retains the same catalytic properties as the naturally occurring enzyme, making it a valuable tool for studying fatty acid metabolism and developing potential treatments for metabolic disorders .
Research on Peroxisomal D3,D2-Enoyl-CoA Isomerase has significant implications for understanding metabolic diseases, particularly those involving fatty acid oxidation defects. The enzyme’s role in energy metabolism makes it a potential target for therapeutic interventions aimed at correcting metabolic imbalances. Additionally, studying the recombinant form of the enzyme provides insights into its structure-function relationships and helps in the development of enzyme replacement therapies .
