GO:0003995 acyl-CoA dehydrogenase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0003995 acyl-CoA dehydrogenase activity catalyzes the oxidation of a 2,3-saturated acyl-CoA to a (2E)-enoyl-CoA, transferring electrons to electron-transfer flavoprotein (ETF).
• The reaction is FAD-dependent and represents the first step of mitochondrial fatty acid beta-oxidation for straight-chain acyl-CoAs.
• Deficiencies in acyl-CoA dehydrogenases cause human diseases including very-long-chain acyl-CoA dehydrogenase deficiency and multiple acyl-CoA dehydrogenase deficiency.
• Medium-chain acyl-CoA dehydrogenase (MCAD) can also act as an isomerase, converting cis-3-enoyl-CoA to trans-2-enoyl-CoA, expanding its catalytic repertoire.
• Acyl-CoA dehydrogenase activity is regulated by nutritional status, including riboflavin availability and starvation.
• ACADL, a long-chain acyl-CoA dehydrogenase, is regulated by the YAP/TEAD4 axis and extracellular matrix mechanics in hepatocellular carcinoma.
Description
Acyl-CoA dehydrogenase activity (GO:0003995) is a fundamental enzymatic activity that catalyzes the alpha,beta-dehydrogenation of acyl-CoA thioesters to generate trans-2-enoyl-CoA, with electrons transferred to electron-transfer flavoprotein (ETF). This reaction constitutes the first oxidative step of mitochondrial fatty acid beta-oxidation and is essential for energy production from fatty acids. The activity is performed by a family of flavin adenine dinucleotide (FAD)-dependent enzymes, each with distinct chain-length specificity, including very-long-chain, long-chain, medium-chain, and short-chain acyl-CoA dehydrogenases. Researchers study acyl-CoA dehydrogenase activity because its dysfunction leads to a group of inherited metabolic disorders known as acyl-CoA dehydrogenase deficiencies, which can present with hypoglycemia, cardiomyopathy, and sudden death. The activity is also implicated in broader metabolic reprogramming in cancer, where enzymes such as ACADL are regulated by mechanical cues and oncogenic pathways. Understanding the molecular mechanism, regulation, and disease relevance of this activity is critical for developing diagnostic and therapeutic strategies. This article provides a comprehensive overview of GO:0003995, covering its definition, catalytic mechanism, key genes, regulatory features, disease associations, and experimental methods for studying it. The content is based on authoritative QuickGO annotation and verified PubMed literature.
acyl-CoA dehydrogenase activity At A Glance
| GO ID | GO:0003995 |
|---|---|
| GO term | acyl-CoA dehydrogenase activity |
| Ontology | molecular_function |
| Synonym | acyl CoA dehydrogenase activity; acyl-CoA reductase activity; acyl coenzyme A dehydrogenase activity; fatty-acyl-CoA dehydrogenase activity; fatty acyl coenzyme A dehydrogenase activity; general acyl CoA dehydrogenase activity |
| Major function | Catalyzes the alpha,beta-dehydrogenation of acyl-CoA thioesters to trans-2-enoyl-CoA, transferring electrons to electron-transfer flavoprotein (ETF) |
| Cofactor | Flavin adenine dinucleotide (FAD) |
| Pathway | Mitochondrial fatty acid beta-oxidation |
| Disease relevance | Deficiencies cause inherited metabolic disorders such as very-long-chain acyl-CoA dehydrogenase deficiency and multiple acyl-CoA dehydrogenase deficiency |
What Is GO:0003995?
According to the Gene Ontology, acyl-CoA dehydrogenase activity (GO:0003995) is defined as the catalysis of the reaction: a 2,3-saturated acyl-CoA + H+ oxidized [electron-transfer flavoprotein] = a (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]. In simpler terms, it is the enzymatic activity that removes two hydrogen atoms from a saturated acyl-CoA molecule to form a double bond, while passing the electrons to electron-transfer flavoprotein (ETF). This activity is synonymous with acyl CoA dehydrogenase activity, acyl-CoA reductase activity, acyl coenzyme A dehydrogenase activity, fatty-acyl-CoA dehydrogenase activity, fatty acyl coenzyme A dehydrogenase activity, and general acyl CoA dehydrogenase activity.
Why Is acyl-CoA dehydrogenase activity Important in Cell Biology?
Acyl-CoA dehydrogenase activity is essential for mitochondrial fatty acid beta-oxidation, the primary pathway for deriving energy from fatty acids during fasting and prolonged exercise. Deficiencies in specific acyl-CoA dehydrogenases are associated with severe human diseases, including very-long-chain acyl-CoA dehydrogenase deficiency, which can cause cardiomyopathy and sudden death, and multiple acyl-CoA dehydrogenase deficiency, which presents with a wide range of symptoms. Beyond inherited disorders, acyl-CoA dehydrogenase activity is increasingly recognized as a metabolic node in cancer, where its regulation impacts lipid metabolism and tumor progression. Therefore, understanding this activity is crucial for diagnosing and treating metabolic diseases and for exploring its role in cancer biology.
• Catalyzes the first step of mitochondrial fatty acid beta-oxidation, a central energy-producing pathway.
• Deficiency of very-long-chain acyl-CoA dehydrogenase causes a severe inherited disorder with cardiomyopathy and hypoglycemia.
• Multiple acyl-CoA dehydrogenase deficiency is a life-threatening condition affecting multiple enzyme activities.
• Medium-chain acyl-CoA dehydrogenase deficiency is a common inherited metabolic disorder identified by newborn screening.
• Acyl-CoA dehydrogenase activity is regulated by riboflavin status and starvation, linking nutrition to metabolic flux.
• MCAD possesses intrinsic isomerase activity, which may protect against toxic intermediates.
• ACADL, a long-chain acyl-CoA dehydrogenase, is regulated by the YAP/TEAD4 pathway and extracellular matrix mechanics in hepatocellular carcinoma.
• The activity is a target for biochemical assays using recombinant electron transfer flavoprotein.
• Understanding the mechanism aids in developing small-molecule modulators for metabolic diseases.
• Acyl-CoA dehydrogenases are potential biomarkers and therapeutic targets in cancer metabolism.
What Happens During acyl-CoA dehydrogenase activity?
Substrate Binding and Orientation
In simple terms: The enzyme grabs a fatty acid molecule that is attached to a carrier called CoA.
The reaction begins with the binding of a 2,3-saturated acyl-CoA substrate to the active site of the acyl-CoA dehydrogenase enzyme. The substrate's acyl chain is positioned near the flavin adenine dinucleotide (FAD) cofactor, which is non-covalently bound to the enzyme. The chain-length specificity of each acyl-CoA dehydrogenase is determined by the size and shape of the substrate-binding pocket, allowing enzymes such as very-long-chain, long-chain, medium-chain, and short-chain acyl-CoA dehydrogenases to act on different fatty acid lengths.
Catalytic Dehydrogenation
In simple terms: The enzyme removes two hydrogen atoms from the fatty acid, creating a double bond.
The catalytic mechanism involves the abstraction of a hydride from the alpha-carbon and a proton from the beta-carbon of the acyl-CoA thioester, resulting in the formation of a trans-2-enoyl-CoA product. This dehydrogenation step is facilitated by the FAD cofactor, which accepts the electrons and becomes reduced (FADH2). The reaction is stereospecific, yielding the (2E)-enoyl-CoA isomer.
Electron Transfer to ETF
In simple terms: The electrons taken from the fatty acid are passed to another protein called ETF.
Following dehydrogenation, the reduced FADH2 transfers its electrons to electron-transfer flavoprotein (ETF), a soluble mitochondrial matrix protein. This electron transfer regenerates the oxidized FAD, allowing the acyl-CoA dehydrogenase to catalyze another round of reaction. The reduced ETF then delivers electrons to the respiratory chain via electron-transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO), ultimately contributing to ATP production.
Isomerase Side Activity of MCAD
In simple terms: Some acyl-CoA dehydrogenases can also rearrange the double bond in certain molecules.
Medium-chain acyl-CoA dehydrogenase (MCAD) exhibits intrinsic isomerase activity, catalyzing the conversion of cis-3-enoyl-CoA to trans-2-enoyl-CoA. This side activity may serve a protective role by detoxifying potentially harmful cis-3-enoyl-CoA intermediates that can arise during beta-oxidation of unsaturated fatty acids. This finding expands the functional repertoire of acyl-CoA dehydrogenases beyond simple dehydrogenation.
Key Genes Involved in GO:0003995 acyl-CoA dehydrogenase activity
The following genes encode proteins that exhibit acyl-CoA dehydrogenase activity or are directly involved in the electron transfer pathway associated with this activity.
| Gene | Major Role | Research Relevance |
|---|---|---|
| ACADVL | Very-long-chain acyl-CoA dehydrogenase; catalyzes dehydrogenation of very-long-chain acyl-CoAs | Mutations cause VLCAD deficiency; genotype-phenotype correlation studied |
| ACADM | Medium-chain acyl-CoA dehydrogenase; catalyzes dehydrogenation of medium-chain acyl-CoAs | Deficiency is a common inherited metabolic disorder; also has isomerase activity |
| ACADL | Long-chain acyl-CoA dehydrogenase; catalyzes dehydrogenation of long-chain acyl-CoAs | Regulated by YAP/TEAD4 and ECM mechanics in hepatocellular carcinoma |
| ACADS | Short-chain acyl-CoA dehydrogenase; catalyzes dehydrogenation of short-chain acyl-CoAs | Deficiency can cause metabolic disorders; studied in riboflavin deficiency |
| ACADSB | Short/branched-chain acyl-CoA dehydrogenase; acts on branched-chain acyl-CoAs | Involved in isoleucine catabolism; deficiency causes metabolic disease |
| ACAD8 | Isobutyryl-CoA dehydrogenase; acts on isobutyryl-CoA | Deficiency leads to isobutyryl-CoA dehydrogenase deficiency |
| ACAD9 | Acyl-CoA dehydrogenase 9; involved in mitochondrial complex I assembly | Deficiency causes mitochondrial complex I deficiency |
| ACAD10 | Acyl-CoA dehydrogenase family member 10; poorly characterized | Potential role in metabolic regulation |
| ACAD11 | Acyl-CoA dehydrogenase family member 11; poorly characterized | Potential role in fatty acid metabolism |
| ETFA | Electron transfer flavoprotein alpha subunit; accepts electrons from acyl-CoA dehydrogenases | Mutations cause multiple acyl-CoA dehydrogenase deficiency |
| ETFB | Electron transfer flavoprotein beta subunit; accepts electrons from acyl-CoA dehydrogenases | Mutations cause multiple acyl-CoA dehydrogenase deficiency |
| ETFDH | Electron transfer flavoprotein-ubiquinone oxidoreductase; transfers electrons to ubiquinone | Mutations cause multiple acyl-CoA dehydrogenase deficiency |
| HADHA | Trifunctional protein alpha subunit; involved in beta-oxidation downstream of acyl-CoA dehydrogenases | Deficiency causes mitochondrial trifunctional protein deficiency |
| HADHB | Trifunctional protein beta subunit; involved in beta-oxidation | Deficiency causes mitochondrial trifunctional protein deficiency |
| CPT2 | Carnitine palmitoyltransferase 2; facilitates entry of long-chain fatty acids into mitochondria | Deficiency causes CPT II deficiency |
| SLC25A20 | Carnitine-acylcarnitine translocase; transports acylcarnitines into mitochondria | Deficiency causes carnitine-acylcarnitine translocase deficiency |
| PPARA | Peroxisome proliferator-activated receptor alpha; regulates fatty acid oxidation genes | Target for modulating acyl-CoA dehydrogenase expression |
| YAP1 | Yes-associated protein 1; regulates ACADL expression via TEAD4 | Involved in mechanical regulation of lipid metabolism in cancer |
How Is acyl-CoA dehydrogenase activity Regulated?
Acyl-CoA dehydrogenase activity is regulated at multiple levels. Nutritionally, riboflavin deficiency reduces the activity of acyl-CoA dehydrogenases in rats, and starvation further modulates this effect. This suggests that FAD availability, derived from riboflavin, is a key determinant of enzyme activity. Transcriptional regulation also plays a role: in hepatocellular carcinoma, the YAP/TEAD4 axis responds to extracellular matrix mechanical cues to regulate ACADL expression, thereby reprogramming lipid metabolism. Additionally, the intrinsic isomerase activity of MCAD may be regulated by substrate availability and may influence metabolic flux.
acyl-CoA dehydrogenase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| ACADVL | Very-long-chain acyl-CoA dehydrogenase deficiency | Knockout or point-mutation knock-in in cell lines or animal models |
| ACADM | Medium-chain acyl-CoA dehydrogenase deficiency | Knockout cells for metabolic assays; patient-derived fibroblasts |
| ETFA/ETFB/ETFDH | Multiple acyl-CoA dehydrogenase deficiency | Knockout or point-mutation models to study electron transfer defects |
| ACADL | Hepatocellular carcinoma lipid metabolism | Overexpression or knockout in cancer cell lines under varying ECM stiffness |
| ACADS | Short-chain acyl-CoA dehydrogenase deficiency | Knockout models to study riboflavin-dependent regulation |
Very-Long-Chain Acyl-CoA Dehydrogenase Deficiency
Very-long-chain acyl-CoA dehydrogenase (VLCAD) deficiency is an inherited disorder caused by mutations in ACADVL, leading to impaired oxidation of long-chain fatty acids. The clinical phenotype correlates with genotype, ranging from severe cardiomyopathy and hypoglycemia in infancy to milder exercise intolerance in adulthood. Early diagnosis and management are critical to prevent metabolic decompensation.
Multiple Acyl-CoA Dehydrogenase Deficiency
Multiple acyl-CoA dehydrogenase deficiency (MADD) is a disorder affecting all acyl-CoA dehydrogenases due to defects in electron transfer flavoprotein (ETF) or ETF-ubiquinone oxidoreductase (ETF-QO). Late-onset MADD can present insidiously with muscle weakness and metabolic abnormalities, making diagnosis challenging. Mutations in ETFA, ETFB, or ETFDH underlie the disease.
Medium-Chain Acyl-CoA Dehydrogenase Deficiency
Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency is one of the most common inherited metabolic disorders, identified by newborn screening using tandem mass spectrometry. It can cause hypoglycemia, lethargy, and seizures during fasting, but early detection and management improve outcomes. The enzyme's intrinsic isomerase activity may modulate disease severity.
Acyl-CoA Dehydrogenase Activity in Cancer
In hepatocellular carcinoma, the long-chain acyl-CoA dehydrogenase ACADL is regulated by the YAP/TEAD4 pathway in response to extracellular matrix mechanics, affecting lipid metabolism and tumor progression. This highlights a role for acyl-CoA dehydrogenase activity beyond inherited metabolic disorders, linking it to cancer cell metabolism and potential therapeutic targeting.
From acyl-CoA dehydrogenase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| What is the effect of ACADVL loss on fatty acid oxidation? | ACADVL knockout cell line (e.g., HEK293 or HepG2) |
| How does a specific ACADM mutation affect enzyme activity? | Point-mutation knock-in of patient variants in cell lines |
| Does restoration of ACADL expression reverse cancer phenotypes? | Knock-in or overexpression of ACADL in hepatocellular carcinoma cells |
| How does riboflavin deficiency alter acyl-CoA dehydrogenase activity? | Knockout of ACADS in cells cultured in riboflavin-deficient media |
| What is the role of ETF subunits in electron transfer? | Knockout of ETFA, ETFB, or ETFDH in cell lines |
| Can MCAD isomerase activity be separated from dehydrogenase activity? | Point mutations in ACADM to abolish isomerase activity |
How to Study the acyl-CoA dehydrogenase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Microplate activity assay with recombinant ETF | Acyl-CoA dehydrogenase enzymatic activity | High-throughput screening of inhibitors or mutants |
| Spectrophotometric assay with DCIP | Dehydrogenation activity | Kinetic characterization of purified enzymes |
| RNA-seq | Gene expression changes | Identifying ACAD gene regulation in cancer or metabolic states |
| CRISPR knockout screening | Genes required for activity or viability | Functional genomics of fatty acid oxidation |
| 13C metabolic flux analysis | Flux through beta-oxidation | Quantifying metabolic reprogramming |
| Tandem mass spectrometry (MS/MS) | Acylcarnitine profiles | Newborn screening for MCAD deficiency |
| Genotype-phenotype correlation | Association of mutations with clinical outcomes | Prognosis and genetic counseling in VLCAD deficiency |
| Enzyme isomerase assay | Isomerase side activity of MCAD | Mechanistic studies of MCAD |
Enzymatic Activity Assays
Acyl-CoA dehydrogenase activity can be measured using a microplate assay with recombinant porcine electron transfer flavoprotein (ETF) as an electron acceptor. This method allows quantitative assessment of enzyme kinetics and inhibition. Alternatively, spectrophotometric assays monitoring the reduction of ETF or artificial electron acceptors like dichlorophenolindophenol (DCIP) are commonly used.
Genetic and Genomic Approaches
CRISPR-Cas9 knockout screens can identify genes required for acyl-CoA dehydrogenase activity and fatty acid oxidation. Transcriptomic profiling, such as RNA-seq, reveals expression changes in ACAD genes under different conditions, including mechanical cues in cancer. Genotype-phenotype correlation studies in patient cohorts help link specific mutations to disease severity.
Metabolic Flux Analysis
Isotope tracing with 13C-labeled fatty acids coupled to mass spectrometry can measure flux through beta-oxidation and assess acyl-CoA dehydrogenase activity in cells and tissues. This approach is valuable for understanding metabolic reprogramming in diseases like cancer.
Newborn Screening and Clinical Diagnostics
Tandem mass spectrometry (MS/MS) of dried blood spots is used to detect acylcarnitine profiles indicative of acyl-CoA dehydrogenase deficiencies, such as MCAD deficiency. This method enables early diagnosis and intervention.
How CRISPR Can Be Used to Study GO:0003995 acyl-CoA dehydrogenase activity
Knockout
CRISPR-Cas9 knockout of ACAD genes (e.g., ACADVL, ACADM, ACADL) in cell lines or animal models enables the study of loss-of-function phenotypes, including impaired fatty acid oxidation and metabolic stress. Knockout models are essential for validating gene function and for drug discovery.
Point Mutation
Introducing patient-specific point mutations (e.g., in ACADVL or ACADM) via CRISPR base editing or homology-directed repair allows researchers to study the molecular consequences of disease-associated variants. These models help establish genotype-phenotype correlations.
Knock-in
Knock-in of tagged versions of acyl-CoA dehydrogenases (e.g., FLAG- or GFP-tagged ACADL) facilitates protein localization, interaction, and activity studies. Knock-in of wild-type or mutant genes can rescue or exacerbate phenotypes in knockout backgrounds.
Overexpression
CRISPR activation (CRISPRa) or lentiviral overexpression of ACAD genes can model increased enzyme activity and its effects on metabolism and disease. Overexpression of ACADL in cancer cells has been used to study its role in tumor suppression.
How EDITGENE Supports acyl-CoA dehydrogenase activity Research
Researchers studying acyl-CoA dehydrogenase activity-related genes often need to determine whether a candidate gene is causally involved in metabolic phenotypes, disease progression, or drug response. EDITGENE provides comprehensive CRISPR-based services to create precisely engineered cell models, enabling functional validation of genes encoding acyl-CoA dehydrogenases and their regulators.
Contact EDITGENE today to design your custom CRISPR model for acyl-CoA dehydrogenase activity research.
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| ACAD10 Knockout HEK293 Cell Line | EDJ-KQ2319 | Human | 80724 | Details Get a Quote |
| ACADM Knockout HEK293 Cell Line | EDJ-KQ3144 | Human | 34 | Details Get a Quote |
| ACADL Knockout HEK293 Cell Line | EDJ-KQ3148 | Human | 33 | Details Get a Quote |
| ACADVL Knockout HEK293 Cell Line | EDJ-KQ3277 | Human | 37 | Details Get a Quote |
| ACADS Knockout HEK293 Cell Line | EDJ-KQ3992 | Human | 35 | Details Get a Quote |
| ACADSB Knockout HEK293 Cell Line | EDJ-KQ3993 | Human | 36 | Details Get a Quote |
| GCDH Knockout HEK293 Cell Line | EDJ-KQ4688 | Human | 2639 | Details Get a Quote |
| IVD Knockout HEK293 Cell Line | EDJ-KQ5012 | Human | 3712 | Details Get a Quote |
| ACAD8 Knockout HEK293 Cell Line | EDJ-KQ8651 | Human | 27034 | Details Get a Quote |
| ACAD9 Knockout HEK293 Cell Line | EDJ-KQ8952 | Human | 28976 | Details Get a Quote |
| ACAD11 Knockout HEK293 Cell Line | EDJ-KQ9989 | Human | 84129 | Details Get a Quote |
| ACADSB Knockout A-549 Cell Line | EDJ-KQ24966 | Human | 36 | Details Get a Quote |
| GCDH Knockout A-549 Cell Line | EDJ-KQ26152 | Human | 2639 | Details Get a Quote |
| IVD Knockout A-549 Cell Line | EDJ-KQ27924 | Human | 3712 | Details Get a Quote |
| IVD Knockout HCT 116 Cell Line | EDJ-KQ27925 | Human | 3712 | Details Get a Quote |
Displaying Records 1 To 15 Of 45 Records
- 1
- 2
- Next Page »
Frequently Asked Questions About acyl-CoA dehydrogenase activity
What is acyl-CoA dehydrogenase activity?
Acyl-CoA dehydrogenase activity (GO:0003995) is the enzymatic activity that catalyzes the dehydrogenation of a 2,3-saturated acyl-CoA to a (2E)-enoyl-CoA, transferring electrons to electron-transfer flavoprotein (ETF).
What genes are involved in acyl-CoA dehydrogenase activity?
Genes encoding acyl-CoA dehydrogenases include ACADVL, ACADM, ACADL, ACADS, ACADSB, ACAD8, ACAD9, ACAD10, and ACAD11, as well as electron transfer genes ETFA, ETFB, and ETFDH.
What diseases are associated with acyl-CoA dehydrogenase deficiency?
Deficiencies cause very-long-chain acyl-CoA dehydrogenase deficiency, medium-chain acyl-CoA dehydrogenase deficiency, and multiple acyl-CoA dehydrogenase deficiency, among others.
How is acyl-CoA dehydrogenase activity measured?
It can be measured using a microplate assay with recombinant electron transfer flavoprotein or spectrophotometric assays monitoring electron acceptor reduction.
What is the role of FAD in acyl-CoA dehydrogenase activity?
FAD is the cofactor that accepts electrons during the dehydrogenation reaction, becoming reduced and then transferring electrons to ETF.
Can acyl-CoA dehydrogenase have isomerase activity?
Yes, medium-chain acyl-CoA dehydrogenase (MCAD) exhibits intrinsic isomerase activity, converting cis-3-enoyl-CoA to trans-2-enoyl-CoA.
How is acyl-CoA dehydrogenase activity regulated?
It is regulated by nutritional status such as riboflavin availability and starvation, and transcriptionally by pathways like YAP/TEAD4 in cancer.
What is the connection between acyl-CoA dehydrogenase and cancer?
ACADL is regulated by the YAP/TEAD4 axis and extracellular matrix mechanics in hepatocellular carcinoma, affecting lipid metabolism and tumor progression.
What model systems are used to study acyl-CoA dehydrogenase activity?
Knockout, point-mutation knock-in, and overexpression cell models, as well as animal models, are used to study gene function and disease mechanisms.
How does newborn screening detect acyl-CoA dehydrogenase deficiencies?
Tandem mass spectrometry (MS/MS) detects abnormal acylcarnitine profiles in dried blood spots, enabling early diagnosis of disorders like MCAD deficiency.
Conclusion
Acyl-CoA dehydrogenase activity (GO:0003995) is a cornerstone of mitochondrial fatty acid beta-oxidation, with critical roles in energy metabolism and human disease. The activity is mediated by a family of FAD-dependent enzymes with distinct substrate specificities, and its dysfunction leads to severe inherited metabolic disorders. Emerging evidence also links acyl-CoA dehydrogenase activity to cancer metabolism and mechanical signaling. Understanding the molecular mechanism, regulation, and disease relevance of this activity provides a foundation for developing diagnostic and therapeutic strategies. Researchers can leverage CRISPR-based models, enzymatic assays, and metabolic profiling to dissect the function of individual acyl-CoA dehydrogenases and their regulators. EDITGENE offers a comprehensive suite of services to support these investigations, from knockout and knock-in cell lines to library screening and bioinformatics analysis.
References
- 1. Andresen BS et al.. 1999. Clear correlation of genotype with disease phenotype in very-long-chain acyl-CoA dehydrogenase deficiency.. Am J Hum Genet 64(2):479-94 PMID: 9973285
- 2. Zhang Y et al.. 2019. An acyl-CoA dehydrogenase microplate activity assay using recombinant porcine electron transfer flavoprotein.. Anal Biochem 581:113332 PMID: 31194945
- 3. Głąb-Jabłońska E et al.. 2025. Medium-chain Acyl-CoA Dehydrogenase Deficiency Identified by MS/MS Newborn Screening Challenges.. J Mother Child 29(1):227-233 PMID: 41346164
- 4. Ross NS et al.. 1987. Acyl-CoA dehydrogenase activity in the riboflavin-deficient rat. Effects of starvation.. Biochem J 244(2):387-91 PMID: 3663132
- 5. Cai J et al.. 2023. Bulk and single-cell transcriptome profiling reveal extracellular matrix mechanical regulation of lipid metabolism reprograming through YAP/TEAD4/ACADL axis in hepatocellular carcinoma.. Int J Biol Sci 19(7):2114-2131 PMID: 37151879
- 6. Zeng J et al.. 2005. Intrinsic isomerase activity of medium-chain acyl-CoA dehydrogenase.. Biochemistry 44(17):6715-22 PMID: 15850406
- 7. Rao NN et al.. 2023. Late-onset multiple acyl-CoA dehydrogenase deficiency: an insidious presentation.. BMJ Case Rep 16(5) PMID: 37217231
- 8. Ghisla S et al.. 2004. Acyl-CoA dehydrogenases. A mechanistic overview.. Eur J Biochem 271(3):494-508 PMID: 14728676
