ACADS encodes short-chain acyl-CoA dehydrogenase (SCAD), a soluble mitochondrial matrix flavoenzyme that catalyzes the initial dehydrogenation reaction of short-chain acyl-CoA beta-oxidation. It converts saturated acyl-CoA substrates to trans-2-enoyl-CoAs and transfers reducing equivalents through its FAD cofactor to electron-transfer flavoprotein. Butyryl-CoA is a characteristic substrate, and the substrate range includes hexanoyl-CoA. The mature enzyme is a homotetramer with one FAD per subunit and is generated by cleavage of an N-terminal mitochondrial targeting peptide. Reduced ACADS activity causes the biochemical defect of short-chain acyl-CoA dehydrogenase deficiency, including accumulation of ethylmalonic acid.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0016937 short-chain fatty acyl-CoA dehydrogenase activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT places short-chain acyl-CoA dehydrogenase activity at ancestral node PTN000097838. Human SCAD directly converts butyryl-CoA to crotonyl-CoA. Reason: The inherited activity agrees with purified human enzyme evidence and the current GO definition. Short-chain describes the acyl substrate range; the term does not require exclusively straight-chain substrates. The human experimental descendant in the PAINT evidence is legitimate support, not circularity. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000097838 SUPPORTS TRANSFER The cached PTHR43884 PAINT table contains the GO:0016937 IBD at this node, including experimental human, rat and bovine descendants. No target-specific loss is evident. Supporting Evidence: PMID:3597357 The products of SCA dehydrogenase/butyryl-CoA, MCA dehydrogenase/octanoyl-CoA, and IV dehydrogenase/isovaleryl-CoA reactions were identified as crotonyl-CoA PMID:3597357 They all utilized electron transfer flavoprotein (ETF) or phenazine methosulfate (PMS) as an electron acceptor. |
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | ACCEPT | Summary: The mitochondrial IBA correctly places ACADS in its core organelle. Reason: The cached PAINT IBD at PTN000856533 supports mitochondrion. Preserve the resolution of this phylogenetic assertion; matrix localization is represented by separate annotations and the core function. A broader but sound ancestral location is not a propagation failure. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000856533 SUPPORTS TRANSFER The cached PAINT IBD explicitly asserts mitochondrion at this node. The inherited organelle location is correct and retained at its original resolution; no node-placement failure is inferred. Supporting Evidence: Reactome:R-HSA-77319 ACADS in the mitochondrial matrix dehydrogenates butanoyl-CoA to form (2E)-butenoyl-CoA (crotonoyl-CoA). |
| GO:0033539 fatty acid beta-oxidation using acyl-CoA dehydrogenase | IBA GO_REF:0000033 | ACCEPT | Summary: The PAINT process annotation places ACADS in fatty acid beta-oxidation using acyl-CoA dehydrogenase. Reason: GO:0033539 denotes a beta-oxidation pathway whose initial oxidation in each cycle uses an acyl-CoA dehydrogenase. ACADS directly performs this reaction for short-chain substrates; it does not catalyze the entire multienzyme pathway. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000097838 SUPPORTS TRANSFER The cached PAINT table contains this process IBD at the same short-chain activity node. Direct human enzyme evidence agrees with inherited participation. Supporting Evidence: PMID:3597357 The products of SCA dehydrogenase/butyryl-CoA, MCA dehydrogenase/octanoyl-CoA, and IV dehydrogenase/isovaleryl-CoA reactions were identified as crotonyl-CoA PMID:8276399 one of five homologous dehydrogenases that catalyze the first reaction in the beta-oxidation of fatty acids |
| GO:0046359 butyrate catabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: The butyrate-catabolism IBA is consistent with SCAD dehydrogenation of activated butyrate, butyryl-CoA. Reason: ACADS performs a catalytic step in butyrate breakdown rather than merely serving as a substrate or being necessary indirectly. This substrate-specific process describes core chemistry even though it overlaps the beta-oxidation annotation. It does not imply oxidation of free butyrate by SCAD. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000097838 SUPPORTS TRANSFER The cached PAINT IBD is grounded in rat evidence and placed at the SCAD activity node. Human butyryl-CoA dehydrogenation supports the inherited function; the number of listed descendants is not an objection. Supporting Evidence: PMID:3597357 The products of SCA dehydrogenase/butyryl-CoA, MCA dehydrogenase/octanoyl-CoA, and IV dehydrogenase/isovaleryl-CoA reactions were identified as crotonyl-CoA Reactome:R-HSA-77319 ACADS in the mitochondrial matrix dehydrogenates butanoyl-CoA to form (2E)-butenoyl-CoA (crotonoyl-CoA). |
| GO:0003995 acyl-CoA dehydrogenase activity | IEA GO_REF:0000120 | MODIFY | Summary: The combined ARBA/InterPro mapping correctly identifies acyl-CoA dehydrogenase activity. Reason: Human SCAD enzymology supports the more informative short-chain child term. The broad mapping is biologically valid; the requested change concerns specificity. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: ARBA:ARBA00026877 SUPPORTS TRANSFER This source maps ACADS to the broad enzyme-family activity. Human substrate evidence supplies short-chain specificity; no erroneous family transfer is alleged. InterPro:IPR006089 SUPPORTS TRANSFER This source maps ACADS to the broad enzyme-family activity. Human substrate evidence supplies short-chain specificity; no erroneous family transfer is alleged. Proposed replacements: short-chain fatty acyl-CoA dehydrogenase activity Supporting Evidence: PMID:3597357 The products of SCA dehydrogenase/butyryl-CoA, MCA dehydrogenase/octanoyl-CoA, and IV dehydrogenase/isovaleryl-CoA reactions were identified as crotonyl-CoA |
| GO:0005739 mitochondrion | IEA GO_REF:0000117 | ACCEPT | Summary: The ARBA mitochondrial annotation agrees with ACADS localization. Reason: The organelle-level electronic assignment is correct and retained at the resolution of the mapped source. Separate matrix annotations provide the finer compartment; they do not require rewriting this ARBA assertion. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00026962 SUPPORTS TRANSFER The traced ARBA source assigns the correct mitochondrial organelle. Retain this mapped resolution; the separately supported matrix location does not imply a rule failure. Supporting Evidence: Reactome:R-HSA-77319 ACADS in the mitochondrial matrix dehydrogenates butanoyl-CoA to form (2E)-butenoyl-CoA (crotonoyl-CoA). |
| GO:0005759 mitochondrial matrix | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular-location mapping places SCAD in the mitochondrial matrix. Reason: This is the specific compartment of the soluble enzyme. UniProt maps SL-0170 and records matrix localization by similarity to bovine ACADS; Reactome independently places the catalytic reaction there. Supporting Evidence: Reactome:R-HSA-77319 ACADS in the mitochondrial matrix dehydrogenates butanoyl-CoA to form (2E)-butenoyl-CoA (crotonoyl-CoA). |
| GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors | IEA GO_REF:0000002 | MODIFY | Summary: InterPro correctly classifies SCAD as an oxidoreductase acting on CH-CH donors. Reason: The reaction removes hydrogen equivalents from acyl-CoA C2-C3 and reduces ETF. Purified human SCAD supports the more specific short-chain acyl-CoA dehydrogenase term, a descendant of this broad oxidoreductase activity. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: InterPro:IPR006091 SUPPORTS TRANSFER This InterPro source contributes a valid broad oxidoreductase mapping. Target enzymology resolves short-chain substrate specificity; no domain loss or incorrect propagation is inferred. InterPro:IPR009075 SUPPORTS TRANSFER This InterPro source contributes a valid broad oxidoreductase mapping. Target enzymology resolves short-chain substrate specificity; no domain loss or incorrect propagation is inferred. InterPro:IPR009100 SUPPORTS TRANSFER This InterPro source contributes a valid broad oxidoreductase mapping. Target enzymology resolves short-chain substrate specificity; no domain loss or incorrect propagation is inferred. InterPro:IPR013786 SUPPORTS TRANSFER This InterPro source contributes a valid broad oxidoreductase mapping. Target enzymology resolves short-chain substrate specificity; no domain loss or incorrect propagation is inferred. InterPro:IPR036250 SUPPORTS TRANSFER This InterPro source contributes a valid broad oxidoreductase mapping. Target enzymology resolves short-chain substrate specificity; no domain loss or incorrect propagation is inferred. InterPro:IPR037069 SUPPORTS TRANSFER This InterPro source contributes a valid broad oxidoreductase mapping. Target enzymology resolves short-chain substrate specificity; no domain loss or incorrect propagation is inferred. InterPro:IPR046373 SUPPORTS TRANSFER This InterPro source contributes a valid broad oxidoreductase mapping. Target enzymology resolves short-chain substrate specificity; no domain loss or incorrect propagation is inferred. Proposed replacements: short-chain fatty acyl-CoA dehydrogenase activity Supporting Evidence: PMID:3597357 The products of SCA dehydrogenase/butyryl-CoA, MCA dehydrogenase/octanoyl-CoA, and IV dehydrogenase/isovaleryl-CoA reactions were identified as crotonyl-CoA PMID:3597357 They all utilized electron transfer flavoprotein (ETF) or phenazine methosulfate (PMS) as an electron acceptor. |
| GO:0016937 short-chain fatty acyl-CoA dehydrogenase activity | IEA GO_REF:0000120 | ACCEPT | Summary: The combined Rhea/EC mapping gives short-chain acyl-CoA dehydrogenase activity. Reason: The mapped short-chain, butanoyl-CoA and pentanoyl-CoA reactions agree with curated UniProt catalytic activity and the directly established human butyryl-CoA reaction. Supporting Evidence: PMID:3597357 The products of SCA dehydrogenase/butyryl-CoA, MCA dehydrogenase/octanoyl-CoA, and IV dehydrogenase/isovaleryl-CoA reactions were identified as crotonyl-CoA |
| GO:0033539 fatty acid beta-oxidation using acyl-CoA dehydrogenase | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA assigns ACADS to fatty acid beta-oxidation using acyl-CoA dehydrogenase. Reason: SCAD directly catalyzes an initial dehydrogenation within this multienzyme pathway. The electronic assignment agrees with human enzymology and the independently reviewed PAINT process assertion. Supporting Evidence: PMID:3597357 The products of SCA dehydrogenase/butyryl-CoA, MCA dehydrogenase/octanoyl-CoA, and IV dehydrogenase/isovaleryl-CoA reactions were identified as crotonyl-CoA PMID:8276399 one of five homologous dehydrogenases that catalyze the first reaction in the beta-oxidation of fatty acids |
| GO:0050660 flavin adenine dinucleotide binding | IEA GO_REF:0000002 | ACCEPT | Summary: Purified human SCAD binds one FAD per subunit. Reason: FAD is the redox cofactor for short-chain acyl-CoA dehydrogenation, so this InterPro assignment describes a core catalytic property. Cofactor binding is incorporated into the catalytic core-function description rather than represented as a second independent function. Supporting Evidence: PMID:3597357 each contains 1 mol of FAD per subunit |
| GO:0070991 medium-chain fatty acyl-CoA dehydrogenase activity | IEA GO_REF:0000116 | KEEP AS NON CORE | Summary: Rhea:43464 maps the curated hexanoyl-CoA reaction to medium-chain fatty acyl-CoA dehydrogenase activity. Reason: The actual GO:0070991 entry includes RHEA:43464. Retain this supported overlapping substrate activity without claiming that SCAD has the complete substrate range or physiological role of ACADM. Short-chain acyl-CoA dehydrogenation remains the defining core activity. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: RHEA:43464 SUPPORTS TRANSFER The GO entry explicitly includes this hexanoyl-CoA reaction, which UniProt P16219 and Reactome attribute to ACADS. The mapping is valid; broad medium-chain substrate competence is not inferred. Supporting Evidence: Reactome:R-HSA-77327 ACADS in the mitochondrial matrix dehydrogenates hexanoyl-CoA to form trans-hex-2-enoyl-CoA. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: BioPlex 2.0 provides an AP-MS association underlying the ACADS-DPEP1 protein-binding annotation. Reason: The full cached study explains affinity purification of tagged baits in HEK293T cells and co-complex detection. The curated ACADS-DPEP1 association is also recorded in UniProt, but no more informative molecular function can be assigned from this association. Remove the generic functional annotation as uninformative; this does not reject the interaction or imply that the two proteins cannot associate. The partner-specific supplemental experimental record was not independently reanalyzed. Supporting Evidence: PMID:28514442 robust affinity purification-mass spectrometry methodology to elucidate protein interaction networks file:human/ACADS/ACADS-uniprot.txt P16219; P16444: DPEP1; NbExp=2; IntAct=EBI-3904404, EBI-749514; |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: BioPlex 3.0 supplies a second IPI protein-binding annotation with DPEP1. Reason: This is the same ACADS-DPEP1 AP-MS association as the BioPlex 2.0 annotation, and UniProt records the pair. No more informative molecular function is supported by the available association evidence. Remove the generic protein-binding annotation as uninformative, using the same criterion for both BioPlex rows. This does not reject the physical association. The BioPlex 3.0 cache lacks complete methods/results and the pair-specific record was not independently reanalyzed; these limits preclude a mechanistic replacement, not this functional-information judgment. Supporting Evidence: PMID:33961781 Through affinity-purification mass spectrometry, we have created two proteome-scale, cell-line-specific interaction networks file:human/ACADS/ACADS-uniprot.txt P16219; P16444: DPEP1; NbExp=2; IntAct=EBI-3904404, EBI-749514; |
| GO:0005739 mitochondrion | IDA GO_REF:0000052 | ACCEPT | Summary: The HPA immunofluorescence annotation correctly reports mitochondrial ACADS. Reason: The current HPA subcellular page calls mitochondria the supported main location. Accept the microscopy-supported organelle assignment without claiming that these images resolve the matrix. HPA also lists uncertain nucleoplasm and centrosome signals, which are not converted into new annotations. Supporting Evidence: Reactome:R-HSA-77319 ACADS in the mitochondrial matrix dehydrogenates butanoyl-CoA to form (2E)-butenoyl-CoA (crotonoyl-CoA). |
| GO:0005759 mitochondrial matrix | ISS GO_REF:0000024 | ACCEPT | Summary: The ISS annotation transfers matrix localization from bovine ACADS, UniProtKB:Q3ZBF6. Reason: The donor is the bovine short-chain acyl-CoA dehydrogenase, and the transferred compartment agrees with the human UniProt matrix assignment and curated ACADS reactions. Supporting Evidence: Reactome:R-HSA-77319 ACADS in the mitochondrial matrix dehydrogenates butanoyl-CoA to form (2E)-butenoyl-CoA (crotonoyl-CoA). |
| GO:0016937 short-chain fatty acyl-CoA dehydrogenase activity | EXP PMID:21237683 Identification and characterization of new long chain acyl-C... | ACCEPT | Summary: The curated EXP assignment of short-chain activity cites He et al. 2011. Reason: Retain the experimental curator's short-chain activity assignment. The cached UniProt record explicitly associates EC 1.3.8.1 with experimental evidence from PMID:21237683, and independent purified human SCAD enzymology in PMID:3597357 confirms short-chain catalysis. The cached abstract focuses on ACAD10/11; it is not used as SCAD-specific experimental proof, and no activity from the paralog assays is reassigned to ACADS. Supporting Evidence: PMID:3597357 The products of SCA dehydrogenase/butyryl-CoA, MCA dehydrogenase/octanoyl-CoA, and IV dehydrogenase/isovaleryl-CoA reactions were identified as crotonyl-CoA file:human/ACADS/ACADS-uniprot.txt EC=1.3.8.1 {ECO:0000269|PubMed:21237683}; |
| GO:0005739 mitochondrion | HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an... | ACCEPT | Summary: The MitoCoP HTP annotation assigns ACADS to the mitochondrial compartment. Reason: The cached full study describes a rigorous multipronged mitochondrial proteome. Its ACADS-specific supplemental entry was not separately reanalyzed; retain the curator-supported organelle assignment at the resolution of this source. The title is not treated as result-bearing evidence, and the HTP row is not recast as a matrix assay. Supporting Evidence: Reactome:R-HSA-77319 ACADS in the mitochondrial matrix dehydrogenates butanoyl-CoA to form (2E)-butenoyl-CoA (crotonoyl-CoA). |
| GO:0003995 acyl-CoA dehydrogenase activity | ISS GO_REF:0000024 | MODIFY | Summary: ISS from bovine ACADS gives the correct general acyl-CoA dehydrogenase activity. Reason: The donor is an orthologous short-chain enzyme, and purified human SCAD directly supports the short-chain child activity. Refine specificity without alleging an orthology or source error. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: UniProtKB:Q3ZBF6 SUPPORTS TRANSFER The live UniProt record identifies Q3ZBF6 as bovine ACADS/SCAD. Transfer of the broad activity is sound, and human enzymology justifies the specific child term. Proposed replacements: short-chain fatty acyl-CoA dehydrogenase activity Supporting Evidence: PMID:3597357 The products of SCA dehydrogenase/butyryl-CoA, MCA dehydrogenase/octanoyl-CoA, and IV dehydrogenase/isovaleryl-CoA reactions were identified as crotonyl-CoA |
| GO:0003995 acyl-CoA dehydrogenase activity | IMP PMID:11134486 Role of common gene variations in the molecular pathogenesis... | MODIFY | Summary: Corydon et al. investigated ACADS genotypes and SCAD activity in fibroblasts from patients selected for ethylmalonic aciduria. Reason: The IMP supports a role in acyl-CoA dehydrogenation. Refine to short-chain activity using the gene-specific study and independent purified human enzyme evidence. The abstract reports variable or moderately reduced activity for common variants; it does not establish universal clinical penetrance or complete loss of activity for those variants. Proposed replacements: short-chain fatty acyl-CoA dehydrogenase activity Supporting Evidence: PMID:11134486 a variable or moderately reduced SCAD activity in fibroblasts PMID:3597357 The products of SCA dehydrogenase/butyryl-CoA, MCA dehydrogenase/octanoyl-CoA, and IV dehydrogenase/isovaleryl-CoA reactions were identified as crotonyl-CoA |
| GO:0016937 short-chain fatty acyl-CoA dehydrogenase activity | ISS GO_REF:0000024 | ACCEPT | Summary: The ISS annotation transfers short-chain acyl-CoA dehydrogenase activity from bovine ACADS. Reason: Bovine Q3ZBF6 is the orthologous enzyme; the transferred activity agrees with direct biochemical evidence for human SCAD. Supporting Evidence: PMID:3597357 The products of SCA dehydrogenase/butyryl-CoA, MCA dehydrogenase/octanoyl-CoA, and IV dehydrogenase/isovaleryl-CoA reactions were identified as crotonyl-CoA |
| GO:0003995 acyl-CoA dehydrogenase activity | IDA PMID:3597357 Purification and properties of short chain acyl-CoA, medium ... | MODIFY | Summary: Finocchiaro et al. purified human liver SCAD and demonstrated butyryl-CoA dehydrogenation with ETF as an electron acceptor. Reason: This IDA establishes the core enzyme activity. Refine the broad acyl-CoA dehydrogenase term to its short-chain child on the basis of the measured substrate/product reaction. Proposed replacements: short-chain fatty acyl-CoA dehydrogenase activity Supporting Evidence: PMID:3597357 The products of SCA dehydrogenase/butyryl-CoA, MCA dehydrogenase/octanoyl-CoA, and IV dehydrogenase/isovaleryl-CoA reactions were identified as crotonyl-CoA PMID:3597357 They all utilized electron transfer flavoprotein (ETF) or phenazine methosulfate (PMS) as an electron acceptor. |
| GO:0033539 fatty acid beta-oxidation using acyl-CoA dehydrogenase | IDA PMID:3597357 Purification and properties of short chain acyl-CoA, medium ... | ACCEPT | Summary: The human liver SCAD reaction directly supports participation in acyl-CoA-dehydrogenase-dependent beta-oxidation. Reason: ACADS performs the initial oxidation of short-chain acyl-CoA within the pathway. The annotation assigns pathway participation, not responsibility for every beta-oxidation reaction. Supporting Evidence: PMID:3597357 The products of SCA dehydrogenase/butyryl-CoA, MCA dehydrogenase/octanoyl-CoA, and IV dehydrogenase/isovaleryl-CoA reactions were identified as crotonyl-CoA PMID:3597357 They all utilized electron transfer flavoprotein (ETF) or phenazine methosulfate (PMS) as an electron acceptor. |
| GO:0005634 nucleus | HDA PMID:21630459 Proteomic characterization of the human sperm nucleus. | UNDECIDED | Summary: The sperm-nucleus proteomics study supports the curator's HDA annotation, but the ACADS-specific full-paper evidence is unavailable. Reason: The abstract reports over 99.9% nuclear purity and absence of mitochondria by light and electron microscopy. It therefore does not justify the previous claim that ACADS detection was almost certainly contamination. Full methods and ACADS peptide-level evidence could not be inspected; retain uncertainty about context-specific nuclear localization without inferring a nuclear function. HPA also reports an uncertain nucleoplasm signal, which is not decisive confirmation. Supporting Evidence: PMID:21630459 isolated to over 99.9% purity without any tail fragments, acrosome or mitochondria |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-77319 | ACCEPT | Summary: Reactome locates ACADS-catalyzed butanoyl-CoA dehydrogenation in the mitochondrial matrix. Reason: The reaction provides target-specific, function-linked support for the matrix as the core compartment. Supporting Evidence: Reactome:R-HSA-77319 ACADS in the mitochondrial matrix dehydrogenates butanoyl-CoA to form (2E)-butenoyl-CoA (crotonoyl-CoA). |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-77327 | ACCEPT | Summary: Reactome locates ACADS-catalyzed hexanoyl-CoA dehydrogenation in the mitochondrial matrix. Reason: This is consistent with the matrix localization of the short-chain enzyme and its documented overlapping C6 substrate activity. Supporting Evidence: Reactome:R-HSA-77327 ACADS in the mitochondrial matrix dehydrogenates hexanoyl-CoA to form trans-hex-2-enoyl-CoA. |
| GO:0005739 mitochondrion | IDA PMID:16729965 Novel localization of OCTN1, an organic cation/carnitine tra... | ACCEPT | Summary: MGI curated mitochondrial localization of ACADS from the OCTN1 localization study. Reason: The abstract focuses on OCTN1 and does not resolve the ACADS assay; indexed publisher text includes SCAD among the study abbreviations, so a wrong-gene claim would be unjustified. Accept the experimental curator's mitochondrial assignment, which agrees with independent ACADS localization evidence. Preserve the source's organelle-level resolution without attributing a matrix result to the unread experiment. Supporting Evidence: Reactome:R-HSA-77319 ACADS in the mitochondrial matrix dehydrogenates butanoyl-CoA to form (2E)-butenoyl-CoA (crotonoyl-CoA). |
| GO:0003995 acyl-CoA dehydrogenase activity | TAS PMID:2565344 Molecular cloning and nucleotide sequence of complementary D... | MODIFY | Summary: Naito et al. cloned human placental SCAD and identified its mitochondrial precursor and mature sequence. Reason: The TAS correctly identifies an acyl-CoA dehydrogenase. The paper names the short-chain enzyme, and independent human enzyme assays support the specific child activity. Do not treat cDNA cloning alone as a new catalytic assay. Proposed replacements: short-chain fatty acyl-CoA dehydrogenase activity Supporting Evidence: PMID:2565344 Complementary DNAs encoding the precursor of human placental short chain acyl-coenzyme A (CoA) dehydrogenase (SCAD) PMID:3597357 The products of SCA dehydrogenase/butyryl-CoA, MCA dehydrogenase/octanoyl-CoA, and IV dehydrogenase/isovaleryl-CoA reactions were identified as crotonyl-CoA |
| GO:0006635 fatty acid beta-oxidation | TAS PMID:8276399 Cloning and characterization of the mouse short-chain acyl-C... | MODIFY | Summary: The mouse SCAD cDNA paper explicitly describes SCAD as catalyzing the first reaction of fatty acid beta-oxidation. Reason: This ortholog paper supplies a valid author statement about SCAD function. The more specific acyl-CoA-dehydrogenase-dependent pathway term captures the mechanism; human enzyme evidence independently corroborates it. Proposed replacements: fatty acid beta-oxidation using acyl-CoA dehydrogenase Supporting Evidence: PMID:8276399 one of five homologous dehydrogenases that catalyze the first reaction in the beta-oxidation of fatty acids PMID:3597357 The products of SCA dehydrogenase/butyryl-CoA, MCA dehydrogenase/octanoyl-CoA, and IV dehydrogenase/isovaleryl-CoA reactions were identified as crotonyl-CoA |
| GO:0006635 fatty acid beta-oxidation | IC PMID:11134486 Role of common gene variations in the molecular pathogenesis... | MODIFY | Summary: The curator inferred fatty acid beta-oxidation from SCAD acyl-CoA dehydrogenase activity in the variant study. Reason: That inference is sound because ACADS catalyzes a pathway reaction. Refine to the acyl-CoA-dehydrogenase-dependent beta-oxidation term, with direct human reaction evidence rather than disease necessity alone. Proposed replacements: fatty acid beta-oxidation using acyl-CoA dehydrogenase Supporting Evidence: PMID:11134486 a variable or moderately reduced SCAD activity in fibroblasts PMID:3597357 The products of SCA dehydrogenase/butyryl-CoA, MCA dehydrogenase/octanoyl-CoA, and IV dehydrogenase/isovaleryl-CoA reactions were identified as crotonyl-CoA |
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Q: Does the curated ACADS-DPEP1 association have a physiological function beyond the AP-MS interaction record?
Experiment: Validate ACADS localization in purified sperm nuclei with peptide-level identification and orthogonal antibody or tagged-protein controls, distinguishing nuclear signal from the mitochondrial compartment.
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