ECHS1 (short-chain enoyl-CoA hydratase 1; mitochondrial enoyl-CoA hydratase, the classic "crotonase"; EC 4.2.1.17) is a soluble homohexameric (dimer of trimers) enzyme of the mitochondrial matrix that catalyzes the second step of the fatty acid beta-oxidation spiral: the reversible addition of water across the double bond of a 2-trans-enoyl-CoA to yield the corresponding (3S)-3-hydroxyacyl-CoA. It hydrates short- and medium-chain enoyl-CoA thioesters (C4 up to C16) with highest catalytic efficiency toward crotonyl-CoA. Beyond fatty acid oxidation, ECHS1 has a broad substrate range that places it at a central node of branched-chain amino acid catabolism: it hydrates valine-pathway intermediates (methacrylyl-CoA to 3-hydroxyisobutyryl-CoA, and acryloyl-CoA), 3-methylcrotonyl-CoA (leucine pathway) and tiglyl-CoA (isoleucine pathway). A slower delta(3)-delta(2)-enoyl-CoA isomerase activity has been inferred by similarity to orthologs. ECHS1 is synthesized with a cleaved N-terminal mitochondrial targeting presequence and is most abundant in liver, muscle and fibroblasts. Biallelic loss-of-function variants cause mitochondrial short-chain enoyl-CoA hydratase 1 deficiency (ECHS1D), a Leigh-like encephalopathy in which neurotoxicity is attributed chiefly to accumulation of reactive valine-pathway intermediates (methacrylyl-CoA/acryloyl-CoA) rather than to the block in fatty acid oxidation per se.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Phylogenetic (IBA) localization to the mitochondrion. ECHS1 is a well-established mitochondrial matrix enzyme, so this is correct but less specific than the matrix annotations. Reason: Correct compartment but subsumed by the more precise mitochondrial matrix annotations (GO:0005759), which better capture where this soluble enzyme acts. |
| GO:0006635 fatty acid beta-oxidation | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic inference that ECHS1 participates in fatty acid beta-oxidation, consistent with its experimentally demonstrated role as the hydratase of the beta-oxidation spiral. Reason: ECHS1 catalyzes the second (hydration) step of mitochondrial short-/medium-chain fatty acid beta-oxidation. This is one of the gene's core biological processes and is also supported by direct experimental evidence (PMID:26251176). Supporting Evidence: PMID:26251176 including mitochondrial short-chain fatty acid Ξ²-oxidation |
| GO:0003824 catalytic activity | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: Root-level molecular function term from InterPro domain mapping. ECHS1 is indeed a catalytic enzyme, but this term is uninformative and fully subsumed by the specific enoyl-CoA hydratase activity annotation. Reason: "catalytic activity" is a high-level placeholder superseded by GO:0004300 enoyl-CoA hydratase activity, which is experimentally supported. |
| GO:0004165 delta(3)-delta(2)-enoyl-CoA isomerase activity | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Secondary enoyl-CoA isomerase activity (EC 5.3.3.8) assigned electronically from the EC/Rhea mapping. In UniProt this activity is annotated only by similarity to the rat ortholog (P14604, ECO:0000250), not experimentally demonstrated for human ECHS1. Reason: Plausible minor activity ("At a lower rate than the hydratase reaction, catalyzes the isomerase reaction"), but inferred by similarity rather than measured in human, so it should not be treated as a core function. Supporting Evidence: PMID:9073515 short chain enoyl-CoA hydratase (ECHS1; EC 4.2.1.17) |
| GO:0004300 enoyl-CoA hydratase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic assignment of the defining EC 4.2.1.17 activity. This is the core molecular function of ECHS1 and is independently confirmed by direct experimental data. Reason: Enoyl-CoA hydratase activity is the central, experimentally validated function of ECHS1 (PMID:26251176); the electronic annotation is correct. Supporting Evidence: PMID:26251176 Human ECHS1 catalyses the hydration of five substrates via different metabolic pathways |
| GO:0005759 mitochondrial matrix | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic localization to the mitochondrial matrix, the correct compartment for this soluble matrix enzyme, consistent with experimental (IDA) evidence. Reason: ECHS1 is a soluble homohexamer of the mitochondrial matrix (UniProt SUBCELLULAR LOCATION); directly supported by IDA evidence (PMID:40056416). |
| GO:0009083 branched-chain amino acid catabolic process | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Electronic assignment that ECHS1 acts in branched-chain amino acid catabolism. ECHS1 hydrates valine- (methacrylyl-CoA), leucine- (3-methylcrotonyl-CoA) and isoleucine- (tiglyl-CoA) pathway intermediates, so this is correct. Reason: Correct, but it is the broad parent of the more specific and experimentally supported L-valine catabolic process (GO:0006574). Retained as a valid non-core annotation. Supporting Evidence: PMID:26251176 branched-chain amino acid catabolic pathways |
| GO:0018812 3-hydroxyacyl-CoA dehydratase activity | IEA GO_REF:0000116 | KEEP AS NON CORE | Summary: RHEA-based assignment (RHEA:16105 etc.) describing the EC 4.2.1.17 reaction written in the dehydratase direction. This is the same chemistry as enoyl-CoA hydratase activity. Reason: Describes the same reversible reaction as the core GO:0004300 annotation, just in the opposite direction; valid but redundant with the hydratase MF. |
| GO:0043956 3-hydroxypropionyl-CoA dehydratase activity | IEA GO_REF:0000116 | ACCEPT | Summary: RHEA assignment for hydration/dehydration of acryloyl-CoA (3-hydroxypropanoyl-CoA <=> acryloyl-CoA + H2O). Acryloyl-CoA is in the experimentally measured substrate panel, so this specific activity is supported (and is duplicated below by an IDA annotation). Reason: ECHS1 hydrates acryloyl-CoA (a valine-pathway intermediate); experimental kinetics (KM=34.04 uM) and an IDA annotation (PMID:26251176) support this specific activity. |
| GO:0120092 (2E)-butenoyl-CoA hydratase activity | IEA GO_REF:0000116 | ACCEPT | Summary: RHEA assignment for hydration of crotonyl-CoA ((2E)-butenoyl-CoA), the highest-affinity and best characterized substrate of ECHS1. Reason: Crotonyl-CoA hydration is the prototypic ECHS1 ("crotonase") reaction, with the highest measured catalytic specificity (KM=12.75 uM); a valid specific child of enoyl-CoA hydratase activity. Supporting Evidence: PMID:26251176 with the highest specificity for crotonyl-CoA |
| GO:0170035 L-amino acid catabolic process | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: Very broad ARBA-derived process term. ECHS1's amino-acid-related role is specifically in branched-chain (valine) catabolism; this generic parent adds no information. Reason: Overly general; superseded by GO:0009083 (branched-chain amino acid catabolic process) and GO:0006574 (L-valine catabolic process). |
| GO:0005515 protein binding | IPI PMID:23416296 ECHS1 interacts with STAT3 and negatively regulates STAT3 si... | KEEP AS NON CORE | Summary: IPI annotation capturing the ECHS1-STAT3 interaction (yeast two-hybrid, GST-pulldown, co-IP), reported to negatively regulate STAT3 signaling. The interaction is real but the bare "protein binding" term is uninformative about function. Reason: Valid experimental interaction but "protein binding" conveys no specific molecular function; possible moonlighting regulatory role, not the metabolic core function. Supporting Evidence: PMID:23416296 we identified enoyl-CoA hydratase short chain 1 (ECHS1) as a novel STAT3 binding protein |
| GO:0005515 protein binding | IPI PMID:24510904 Unbiased screen for interactors of leucine-rich repeat kinas... | KEEP AS NON CORE | Summary: IPI annotation from an unbiased LRRK2 interactor screen in which ECHS1 appeared as a hit. No dedicated functional follow-up establishes a metabolic role for this interaction. Reason: Bare "protein binding" from a large-scale interactome screen; uninformative and not a core function. |
| GO:0005515 protein binding | IPI PMID:24947832 Differential protein-protein interactions of LRRK1 and LRRK2... | KEEP AS NON CORE | Summary: IPI annotation from a LRRK1/LRRK2 differential interactome study listing ECHS1 as an interactor. Reason: Uninformative "protein binding" from an interactome dataset; retained but non-core. |
| GO:0005515 protein binding | IPI PMID:31046837 Parkinson's disease-associated LRRK2-G2019S mutant acts thro... | KEEP AS NON CORE | Summary: IPI annotation associated with a study of LRRK2-G2019S/SERCA-mediated ER stress in astrocytes; ECHS1 is recorded as a LRRK2 interactor. Reason: Uninformative "protein binding"; no specific molecular function for ECHS1 is established. |
| GO:0006574 L-valine catabolic process | IEA GO_REF:0000107 | ACCEPT | Summary: Orthology-based (Ensembl Compara) transfer of L-valine catabolic process. ECHS1 hydrates the valine-pathway intermediate methacrylyl-CoA, and its deficiency is defined as an inborn error of valine metabolism. Reason: A core biological process for ECHS1; also supported by direct experimental (IMP) evidence (PMID:40056416) and by the disease phenotype (an inborn error affecting valine metabolism). Supporting Evidence: PMID:26251176 harbouring defective valine catabolic and Ξ²-oxidation pathways |
| GO:0006635 fatty acid beta-oxidation | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic assignment of fatty acid beta-oxidation, consistent with the core function and with experimental evidence. Reason: ECHS1 is the hydratase of the short/medium-chain beta-oxidation spiral; duplicate of the experimentally supported BP annotation. |
| GO:0006635 fatty acid beta-oxidation | TAS Reactome:R-HSA-77310 | ACCEPT | Summary: Reactome (TAS) annotation placing ECHS1 in the beta-oxidation of lauroyl-CoA to decanoyl-CoA. Correct pathway membership; one of several chain-length-specific Reactome steps redundant with the core BP annotation. Reason: Accurately reflects ECHS1's role in the fatty acid beta-oxidation pathway. |
| GO:0006635 fatty acid beta-oxidation | TAS Reactome:R-HSA-77346 | ACCEPT | Summary: Reactome (TAS) annotation for beta-oxidation of decanoyl-CoA to octanoyl-CoA. Reason: Correct pathway membership; redundant with the core fatty acid beta-oxidation annotation. |
| GO:0006635 fatty acid beta-oxidation | TAS Reactome:R-HSA-77348 | ACCEPT | Summary: Reactome (TAS) annotation for beta-oxidation of octanoyl-CoA to hexanoyl-CoA. Reason: Correct pathway membership; redundant with the core fatty acid beta-oxidation annotation. |
| GO:0006635 fatty acid beta-oxidation | TAS Reactome:R-HSA-77350 | ACCEPT | Summary: Reactome (TAS) annotation for beta-oxidation of hexanoyl-CoA to butanoyl-CoA. Reason: Correct pathway membership; redundant with the core fatty acid beta-oxidation annotation. |
| GO:0006635 fatty acid beta-oxidation | TAS Reactome:R-HSA-77352 | ACCEPT | Summary: Reactome (TAS) annotation for beta-oxidation of butanoyl-CoA to acetyl-CoA (the shortest-chain step, with crotonyl-CoA as the enoyl-CoA substrate). Reason: Correct pathway membership; this final short-chain step uses crotonyl-CoA, ECHS1's best substrate. Redundant with the core fatty acid beta-oxidation annotation. |
| GO:0009083 branched-chain amino acid catabolic process | TAS Reactome:R-HSA-70895 | KEEP AS NON CORE | Summary: Reactome (TAS) placement of ECHS1 in branched-chain amino acid catabolism, consistent with its hydration of valine/leucine/isoleucine pathway intermediates. Reason: Correct but broad; the specific valine catabolism term is the more informative core BP. |
| GO:0004300 enoyl-CoA hydratase activity | EXP PMID:26251176 Clinical, biochemical and metabolic characterisation of a mi... | ACCEPT | Summary: Experimental (EXP) annotation of the defining enoyl-CoA hydratase activity, based on purified human ECHS1 assayed against multiple enoyl-CoA substrates. Reason: Direct experimental demonstration of the core molecular function of ECHS1. Supporting Evidence: PMID:26251176 we purified human ECHS1, and determined the substrate specificity of ECHS1 for five substrates via different metabolic pathways |
| GO:0004300 enoyl-CoA hydratase activity | TAS Reactome:R-HSA-77256 | ACCEPT | Summary: Reactome (TAS) annotation of enoyl-CoA hydratase activity for a specific beta-oxidation reaction (2-trans-dodecenoyl-CoA hydration). Reason: Correct molecular function; one of several Reactome reaction-level annotations redundant with the experimentally supported core MF. |
| GO:0004300 enoyl-CoA hydratase activity | TAS Reactome:R-HSA-77314 | ACCEPT | Summary: Reactome (TAS) enoyl-CoA hydratase activity for crotonoyl-CoA hydration. Reason: Correct molecular function; redundant with the core enoyl-CoA hydratase annotation. |
| GO:0004300 enoyl-CoA hydratase activity | TAS Reactome:R-HSA-77325 | ACCEPT | Summary: Reactome (TAS) enoyl-CoA hydratase activity for trans-hex-2-enoyl-CoA hydration. Reason: Correct molecular function; redundant with the core enoyl-CoA hydratase annotation. |
| GO:0004300 enoyl-CoA hydratase activity | TAS Reactome:R-HSA-77333 | ACCEPT | Summary: Reactome (TAS) enoyl-CoA hydratase activity for trans-oct-2-enoyl-CoA hydration. Reason: Correct molecular function; redundant with the core enoyl-CoA hydratase annotation. |
| GO:0004300 enoyl-CoA hydratase activity | TAS Reactome:R-HSA-77344 | ACCEPT | Summary: Reactome (TAS) enoyl-CoA hydratase activity for trans-dec-2-enoyl-CoA hydration. Reason: Correct molecular function; redundant with the core enoyl-CoA hydratase annotation. |
| GO:0004300 enoyl-CoA hydratase activity | TAS Reactome:R-HSA-9916717 | ACCEPT | Summary: Reactome (TAS) enoyl-CoA hydratase activity within the ECHS1-deficiency disease pathway (synthesis of beta-hydroxyisobutyryl-CoA from methacrylyl-CoA in valine catabolism). Reason: Correct molecular function applied in the valine-catabolism context; redundant with the core enoyl-CoA hydratase annotation. |
| GO:0019477 L-lysine catabolic process | IMP PMID:37198486 Lysine catabolism reprograms tumour immunity through histone... | KEEP AS NON CORE | Summary: IMP annotation derived from a glioma study showing that ECHS1 is the crotonyl-CoA hydratase whose downregulation accumulates crotonyl-CoA (a lysine-catabolism intermediate produced via GCDH) and drives histone H4 lysine crotonylation. ECHS1 consumes crotonyl-CoA rather than performing a dedicated lysine-degradation step, so this placement reflects its action on a shared crotonyl-CoA pool. Reason: Curator-assigned from experimental (full-text) evidence; deferred to per guidelines. Retained as non-core because ECHS1's connection to lysine catabolism is via the shared crotonyl-CoA metabolite, not a canonical lysine-degradation reaction. Supporting Evidence: PMID:37198486 downregulation of the crotonyl-CoA hydratase enoyl-CoA hydratase short chain 1 (ECHS1), leading to accumulation of intracellular crotonyl-CoA and histone H4 lysine crotonylation |
| GO:0005739 mitochondrion | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Immunofluorescence-based (IDA, HPA) mitochondrial localization. Correct but less precise than the matrix annotation. Reason: Subsumed by the more specific mitochondrial matrix localization. |
| GO:0005759 mitochondrial matrix | IDA PMID:40056416 Ectopic protein lysine methacrylation contributes to defects... | ACCEPT | Summary: Direct experimental (IDA) localization of ECHS1 to the mitochondrial matrix, the precise compartment for this soluble homohexameric enzyme. Reason: Best-supported and most specific subcellular localization; this is the core location of ECHS1. |
| GO:0006574 L-valine catabolic process | IMP PMID:40056416 Ectopic protein lysine methacrylation contributes to defects... | ACCEPT | Summary: Direct experimental (IMP) evidence that ECHS1 acts in valine catabolism: its loss (like loss of the downstream enzyme HIBCH) elevates lysine methacrylation, reflecting build-up of the valine-pathway intermediate methacrylyl-CoA that ECHS1 normally hydrates. Reason: A core biological process of ECHS1, supported by genetic loss-of-function evidence and consistent with ECHS1 deficiency being an inborn error of valine metabolism. Supporting Evidence: PMID:40056416 Elevated lysine methacrylation (Kmea) is observed in both HIBCH- and ECHS1-deficient cells and fly tissues |
| GO:0043956 3-hydroxypropionyl-CoA dehydratase activity | IDA PMID:26251176 Clinical, biochemical and metabolic characterisation of a mi... | ACCEPT | Summary: Direct experimental (IDA) annotation of acryloyl-CoA hydration / 3-hydroxypropionyl-CoA dehydration, one of the five substrate reactions measured for purified human ECHS1. Reason: Experimentally measured specific activity (acryloyl-CoA, KM=34.04 uM); a valid specific child of enoyl-CoA hydratase activity relevant to valine/propionate metabolism. Supporting Evidence: PMID:26251176 Human ECHS1 catalyses the hydration of five substrates via different metabolic pathways |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-9916717 | ACCEPT | Summary: Reactome (TAS) mitochondrial matrix localization within the ECHS1-deficiency pathway. Reason: Correct, specific localization; consistent with the IDA evidence. |
| GO:0005739 mitochondrion | HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an... | KEEP AS NON CORE | Summary: High-throughput (HTP) detection of ECHS1 in a high-confidence human mitochondrial proteome. Confirms mitochondrial localization at lower specificity than the matrix term. Reason: Supports mitochondrial localization but is subsumed by the matrix annotation. |
| GO:0004300 enoyl-CoA hydratase activity | IDA PMID:26251176 Clinical, biochemical and metabolic characterisation of a mi... | ACCEPT | Summary: Direct experimental (IDA) demonstration of enoyl-CoA hydratase activity using purified human ECHS1, the strongest evidence for the gene's core molecular function. Reason: Definitive experimental support for the core enoyl-CoA hydratase activity. Supporting Evidence: PMID:26251176 we purified human ECHS1, and determined the substrate specificity of ECHS1 for five substrates |
| GO:0006635 fatty acid beta-oxidation | IDA PMID:26251176 Clinical, biochemical and metabolic characterisation of a mi... | ACCEPT | Summary: Direct experimental (IDA) evidence for ECHS1's role in fatty acid beta-oxidation, based on hydratase activity toward beta-oxidation enoyl-CoA substrates and the deficiency phenotype affecting the beta-oxidation pathway. Reason: A core biological process; experimentally supported. Supporting Evidence: PMID:26251176 including mitochondrial short-chain fatty acid Ξ²-oxidation |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-70870 | ACCEPT | Summary: Reactome (TAS) mitochondrial matrix localization (methacrylyl-CoA hydration reaction). Reason: Correct, specific localization; consistent with experimental evidence. |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-77256 | ACCEPT | Summary: Reactome (TAS) mitochondrial matrix localization (a beta-oxidation hydration reaction). Reason: Correct, specific localization; redundant with other matrix annotations. |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-77314 | ACCEPT | Summary: Reactome (TAS) mitochondrial matrix localization (crotonoyl-CoA hydration reaction). Reason: Correct, specific localization; redundant with other matrix annotations. |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-77325 | ACCEPT | Summary: Reactome (TAS) mitochondrial matrix localization (hex-2-enoyl-CoA hydration reaction). Reason: Correct, specific localization; redundant with other matrix annotations. |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-77333 | ACCEPT | Summary: Reactome (TAS) mitochondrial matrix localization (oct-2-enoyl-CoA hydration reaction). Reason: Correct, specific localization; redundant with other matrix annotations. |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-77344 | ACCEPT | Summary: Reactome (TAS) mitochondrial matrix localization (dec-2-enoyl-CoA hydration reaction). Reason: Correct, specific localization; redundant with other matrix annotations. |
| GO:0005515 protein binding | IPI PMID:14557246 AIP is a mitochondrial import mediator that binds to both im... | KEEP AS NON CORE | Summary: IPI annotation from a study of the mitochondrial import mediator AIP (which binds Tom20 and preproteins). ECHS1 features as a mitochondrial import substrate/preprotein rather than a functional partner. Reason: Uninformative "protein binding"; reflects ECHS1's status as an imported matrix preprotein, not a molecular function. |
| GO:0005739 mitochondrion | TAS PMID:16130169 Proteomics of human umbilical vein endothelial cells applied... | KEEP AS NON CORE | Summary: TAS mitochondrial localization from a HUVEC proteomics study. Correct compartment, low specificity. Reason: Subsumed by the more specific mitochondrial matrix localization. |
| GO:0004300 enoyl-CoA hydratase activity | TAS PMID:9073515 Human mitochondrial enoyl-CoA hydratase gene (ECHS1): struct... | ACCEPT | Summary: TAS annotation of enoyl-CoA hydratase activity from the gene-cloning paper, which describes ECHS1 as catalyzing the second step of beta-oxidation (EC 4.2.1.17). Reason: Correct core molecular function; consistent with the experimental IDA/EXP evidence. Supporting Evidence: PMID:9073515 is catalyzed by short chain enoyl-CoA hydratase (ECHS1; EC 4.2.1.17) |
| GO:0006635 fatty acid beta-oxidation | TAS PMID:9073515 Human mitochondrial enoyl-CoA hydratase gene (ECHS1): struct... | ACCEPT | Summary: TAS annotation of fatty acid beta-oxidation from the cloning paper, which identifies ECHS1 as catalyzing the second step of mitochondrial fatty acid beta-oxidation. Reason: Correct core biological process; consistent with experimental evidence. Supporting Evidence: PMID:9073515 The second step in mitochondrial fatty acid beta-oxidation is catalyzed by short |
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Download this section (compressed HTML)Q: Is ECHS1's reported negative regulation of STAT3 signaling (PMID:23416296) a genuine moonlighting function distinct from its hydratase activity, and does it occur outside the mitochondrial matrix?
Q: Should the L-lysine catabolic process annotation (GO:0019477) be retained, given that ECHS1's connection to lysine catabolism is via consumption of the shared crotonyl-CoA pool rather than a dedicated lysine-degradation reaction?
Q: To what extent is ECHS1 deficiency neurotoxicity driven by accumulation of reactive valine-pathway intermediates (methacrylyl-CoA/acryloyl-CoA) and ectopic protein lysine methacrylation versus the loss of beta-oxidation flux?
Experiment: Measure in vitro hydratase kinetics of purified recombinant human ECHS1 against the full panel of branched-chain enoyl-CoA substrates (methacrylyl-CoA, 3-methylcrotonyl-CoA, tiglyl-CoA, acryloyl-CoA) alongside crotonyl-CoA to quantify its relative contribution to each amino acid catabolic pathway.
Hypothesis: ECHS1 is the principal short-chain enoyl-CoA hydratase for valine-pathway intermediates, explaining why its deficiency presents primarily as an inborn error of valine metabolism.
Experiment: In ECHS1-null cells and patient fibroblasts, perform metabolomic tracing of valine and fatty-acid carbon to determine which accumulating thioester (methacrylyl-CoA vs acryloyl-CoA) most strongly correlates with mitochondrial dysfunction and protein methacrylation.
Hypothesis: Accumulation of methacrylyl-CoA and consequent ectopic lysine methacrylation, rather than the beta-oxidation block, is the principal driver of the ECHS1-deficiency phenotype.
Experiment: Test whether the slower delta(3)-delta(2)-enoyl-CoA isomerase activity inferred by similarity is detectable for purified human ECHS1 using 3-enoyl-CoA substrates.
Hypothesis: Human ECHS1 retains a low-level enoyl-CoA isomerase activity analogous to its rodent ortholog, supporting the EC 5.3.3.8 annotation.
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