GO:0008410 CoA-transferase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0008410 (CoA-transferase activity) describes enzymes that move a coenzyme A (CoA) group from a donor molecule to an acceptor molecule, a central reaction in ketone body, fatty acid, and amino acid metabolism.
• The best-characterized human CoA-transferase is OXCT1 (SCOT), a mitochondrial enzyme that catalyzes the reversible transfer of CoA from succinyl-CoA to acetoacetate, the rate-limiting step of ketolysis.
• OXCT1 is not only a metabolic enzyme; it also functions as a succinyltransferase that modifies proteins such as LACTB, linking CoA-transferase activity directly to hepatocellular carcinoma progression.
• SUCLA2 succinylates and activates OXCT1, creating a regulatory axis that promotes ketolysis and liver tumor growth.
• Beyond OXCT1, human succinyl-CoA:glutarate-CoA transferase (SUGCT) is a putative genetic modifier of glutaric aciduria type 1, showing that CoA-transferase dysfunction can cause or modify inherited metabolic disease.
• CoA-transferase activity is found across all domains of life, from bacterial methylaspartate cycle enzymes to invertebrate muscle acyl-CoA transferases, making it a conserved and experimentally tractable target.
Description
CoA-transferase activity (GO:0008410) is a molecular function defined as the catalysis of the transfer of a coenzyme A (CoA) group from one compound (donor) to another (acceptor). This reaction is chemically distinct from CoA ligation or hydrolysis: instead of consuming ATP to attach CoA to a carboxylate, a CoA-transferase uses a thioester-linked donor (such as succinyl-CoA) to generate a new thioester-linked product (such as acetoacetyl-CoA). Because thioester bonds are high-energy linkages, CoA-transferases can operate reversibly and are often used by cells to conserve energy while redistributing metabolic intermediates. In humans, the most studied CoA-transferase is OXCT1 (also known as SCOT), a mitochondrial matrix enzyme that catalyzes the transfer of CoA from succinyl-CoA to acetoacetate, producing acetoacetyl-CoA and succinate. This reaction is the committing step of ketone body utilization (ketolysis) and is essential for tissues such as the brain, heart, and skeletal muscle to use ketone bodies as fuel during fasting or ketogenic states. Recent work has shown that OXCT1 also possesses a succinyltransferase activity that modifies LACTB, directly connecting CoA-transferase chemistry to tumor biology. CoA-transferase activity is not limited to ketone metabolism. Human succinyl-CoA:glutarate-CoA transferase (SUGCT) uses succinyl-CoA to activate glutarate, and variants in this enzyme are considered genetic modifiers of glutaric aciduria type 1. Bacterial and archaeal CoA-transferases participate in the methylaspartate cycle and oxidative tricarboxylic acid (TCA) cycles, while invertebrate enzymes such as 2-methylbutyryl-CoA:succinate acyl-CoA transferase support muscle energy metabolism. Thus, GO:0008410 represents a conserved and medically relevant enzymatic function that bridges basic metabolism, inherited disease, and cancer.
CoA-transferase activity At A Glance
| GO ID | GO:0008410 |
|---|---|
| GO term | CoA-transferase activity |
| Ontology | molecular_function |
| Synonym | (none) |
| Definition | Catalysis of the transfer of a coenzyme A (CoA) group from one compound (donor) to another (acceptor). |
| Major function | Transfer of a CoA group between donor and acceptor substrates, enabling thioester interconversion in ketone body, fatty acid, and amino acid metabolism. |
| Representative human enzyme | OXCT1 (SCOT), a mitochondrial ketone body-utilizing CoA-transferase. |
| Representative disease link | OXCT1 in hepatocellular carcinoma and SUGCT as a modifier of glutaric aciduria type 1. |
| Conservation | Found in bacteria, archaea, invertebrates, and mammals, including methylaspartate cycle and TCA cycle-related enzymes. |
What Is GO:0008410?
CoA-transferase activity (GO:0008410) is the catalysis of the transfer of a coenzyme A (CoA) group from one compound (the donor) to another compound (the acceptor). In practical terms, an enzyme with this activity takes a CoA molecule that is attached to a donor substrate via a thioester bond and moves it onto an acceptor substrate, forming a new thioester-linked product. The reaction does not require ATP hydrolysis; instead, the energy of the donor thioester bond drives the transfer. A classic example is the OXCT1 reaction, in which succinyl-CoA (donor) transfers its CoA group to acetoacetate (acceptor), yielding succinate and acetoacetyl-CoA. Another example is SUGCT, which transfers CoA from succinyl-CoA to glutarate. Because the reaction is reversible, CoA-transferases can also generate donor thioesters from acceptor thioesters depending on substrate concentrations and cellular metabolic state.
Why Is CoA-transferase activity Important in Cell Biology?
CoA-transferase activity is important because it sits at the intersection of energy metabolism, inherited metabolic disease, and cancer. The human enzyme OXCT1 uses this activity to commit ketone bodies to oxidation, which is essential for extrahepatic tissues during fasting and ketogenic diets. Loss of OXCT1 function causes succinyl-CoA:3-ketoacid CoA transferase deficiency, a disorder of ketone body utilization, and OXCT1 dysregulation has been linked to hepatocellular carcinoma growth and immune evasion. Separately, SUGCT uses CoA-transferase activity to metabolize glutarate, and its variants are considered genetic modifiers of glutaric aciduria type 1, a severe neurometabolic disorder. In microbes, CoA-transferases support the methylaspartate cycle and oxidative TCA cycle, making them relevant to microbial physiology and biotechnology. In invertebrates, acyl-CoA transferases support muscle energy metabolism, illustrating the broad biological reach of this enzyme class. For researchers, GO:0008410 provides a precise functional annotation that can be used to interpret genome-scale screens, metabolic flux data, and disease variant effects.
• Defines the committing step of ketone body utilization in humans through OXCT1, affecting brain, heart, and skeletal muscle energy homeostasis.
• Links directly to hepatocellular carcinoma: OXCT1 succinylates LACTB and promotes tumor growth, while SUCLA2 activates OXCT1 to drive ketolysis.
• Modulates antitumor immunity: targeting OXCT1-mediated ketone metabolism reprograms macrophages and promotes CD8+ T cell responses in hepatocellular carcinoma.
• Explains the biochemical basis of succinyl-CoA:3-ketoacid CoA transferase deficiency and other ketolysis disorders.
• Identifies SUGCT as a putative genetic modifier of glutaric aciduria type 1, a severe inherited neurometabolic disease.
• Supports microbial metabolism, including the methylaspartate cycle in Haloarcula hispanica and the oxidative TCA cycle in Desulfurella acetivorans.
• Provides a target for metabolic engineering and antibiotic discovery in bacteria and archaea.
• Enables interpretation of invertebrate muscle energy metabolism through 2-methylbutyryl-CoA:succinate acyl-CoA transferase.
• Offers a reversible thioester interconversion mechanism that can be exploited in synthetic biology and biocatalysis.
• Serves as a functional annotation node (GO:0008410) for enrichment analysis of metabolic and cancer transcriptomes.
Molecular Mechanism of CoA-transferase activity
Donor thioester binding and acceptor recognition
In simple terms: The enzyme first grabs a CoA-carrying donor molecule and positions the acceptor molecule nearby.
CoA-transferases bind a donor thioester, typically succinyl-CoA, in a pocket that positions the thioester carbonyl for nucleophilic attack. The acceptor substrate, such as acetoacetate or glutarate, is then bound in an adjacent site so that its carboxylate can attack the donor thioester. In OXCT1, this step is the committing event of ketolysis, and in SUGCT it activates glutarate for further metabolism. The enzyme does not require ATP; the thioester bond of the donor provides the necessary energy.
Ping-pong and ternary complex catalytic mechanisms
In simple terms: The CoA group is passed from donor to acceptor, sometimes through a temporary enzyme-CoA intermediate.
CoA-transferases can use a ping-pong mechanism in which the CoA group is transiently transferred to an active-site residue before being passed to the acceptor, or a ternary complex mechanism in which donor and acceptor are bound simultaneously. Structural and kinetic studies of human SUGCT support a mechanism in which succinyl-CoA and glutarate are coordinated for direct CoA transfer. For OXCT1, the reaction is reversible and can generate succinyl-CoA from acetoacetyl-CoA depending on substrate availability. This reversibility allows CoA-transferases to buffer cellular thioester pools.
Succinylation and post-translational regulation
In simple terms: OXCT1 can also attach succinyl groups to other proteins, which changes their behavior.
Beyond classical CoA transfer, OXCT1 functions as a succinyltransferase that succinylates LACTB, and this modification contributes to hepatocellular carcinoma progression. SUCLA2 succinylates and activates OXCT1, forming a regulatory axis that promotes ketolysis and liver tumor growth. These findings show that CoA-transferase activity can be coupled to protein succinylation, expanding the functional output of GO:0008410 beyond small-molecule metabolism. This dual role makes OXCT1 a node where metabolic flux and post-translational modification intersect.
Substrate specificity and metabolic context
In simple terms: Different CoA-transferases prefer different donor and acceptor molecules, fitting them into specific metabolic pathways.
OXCT1 prefers succinyl-CoA as donor and acetoacetate as acceptor, which commits ketone bodies to oxidation. SUGCT uses succinyl-CoA to transfer CoA to glutarate, a reaction relevant to glutaric aciduria type 1. Bacterial and archaeal enzymes such as succinyl-CoA:mesaconate CoA-transferase and succinyl-CoA:acetate CoA-transferase use related chemistry in the methylaspartate cycle and oxidative TCA cycle. Invertebrate 2-methylbutyryl-CoA:succinate acyl-CoA transferase supports muscle energy metabolism, showing that acceptor specificity can vary widely across species.
Tissue distribution and physiological roles
In simple terms: Some CoA-transferases are used mainly in certain tissues, such as the heart, brain, or liver.
OXCT1 is expressed in extrahepatic tissues such as heart, brain, and skeletal muscle, where it enables ketone body utilization during fasting. In hepatocellular carcinoma, OXCT1 expression and activity support tumor growth and influence macrophage polarization and CD8+ T cell responses. SUGCT is relevant to glutarate metabolism and inherited disease risk. Microbial CoA-transferases are expressed under specific growth conditions, such as growth on acetate or methylaspartate. This tissue- and condition-specific expression determines the physiological impact of GO:0008410 in different organisms.
Key Genes Involved in GO:0008410 CoA-transferase activity
The following genes and proteins represent the main experimentally characterized CoA-transferases and their regulators across human, microbial, and invertebrate systems.
| Gene | Major Role | Research Relevance |
|---|---|---|
| OXCT1 | Mitochondrial succinyl-CoA:3-ketoacid CoA transferase that commits ketone bodies to oxidation | Central to ketolysis, hepatocellular carcinoma growth, and macrophage antitumor immunity |
| SUCLA2 | Succinyl-CoA ligase subunit that succinylates and activates OXCT1 | Regulates ketolysis and liver tumor growth through OXCT1 activation |
| LACTB | Substrate of OXCT1 succinyltransferase activity | Succinylation of LACTB contributes to hepatocellular carcinoma progression |
| SUGCT | Succinyl-CoA:glutarate-CoA transferase that activates glutarate | Putative genetic modifier of glutaric aciduria type 1 |
| SUCLA2-OXCT1 axis | Regulatory axis linking succinyl-CoA metabolism to ketolysis | Target for understanding liver tumor metabolism |
| Mesaconate CoA-transferase | Bacterial enzyme of the methylaspartate cycle in Haloarcula hispanica | Model for archaeal carbon metabolism and enzyme evolution |
| Mesaconyl-CoA hydratase | Bacterial enzyme acting with mesaconate CoA-transferase | Complements CoA-transferase studies in the methylaspartate cycle |
| Succinyl-CoA:acetate CoA-transferase | Bacterial enzyme functioning in the oxidative TCA cycle of Desulfurella acetivorans | Model for TCA cycle variants in bacteria |
| 2-Methylbutyryl-CoA:succinate acyl-CoA transferase | Invertebrate muscle enzyme in Ascaris suum | Model for invertebrate energy metabolism |
| SCOT (OXCT1 alias) | Alternative name for OXCT1 in ketone body metabolism | Used in clinical and biochemical literature on ketolysis |
| Acetoacetate | Acceptor substrate for OXCT1 | Radiolabeled acetoacetate is used to trace ketone body metabolism |
| Succinyl-CoA | Donor substrate for many CoA-transferases | Central thioester donor in ketolysis and glutarate metabolism |
| Acetoacetyl-CoA | Product of OXCT1 reaction | Intermediate of ketone body oxidation |
| Glutarate | Acceptor substrate for SUGCT | Relevant to glutaric aciduria type 1 |
| Succinate | Product of CoA transfer from succinyl-CoA | Links CoA-transferase activity to TCA cycle flux |
| CD8+ T cells | Immune effectors influenced by OXCT1-mediated ketone metabolism | Readout for antitumor immunity in hepatocellular carcinoma |
| Macrophages | Immune cells reprogrammed by targeting OXCT1-mediated ketone metabolism | Model for tumor microenvironment studies |
| Haloarcula hispanica enzymes | Archaeal CoA-transferase and hydratase pair | Comparative model for CoA-transferase diversity |
How Is CoA-transferase activity Regulated?
CoA-transferase activity is regulated at multiple levels. In humans, OXCT1 is post-translationally activated by succinylation mediated by SUCLA2, which couples succinyl-CoA availability to ketolysis and liver tumor growth. OXCT1 expression and activity are also influenced by the metabolic state of the cell, with high ketolytic flux in extrahepatic tissues during fasting. In hepatocellular carcinoma, OXCT1-mediated ketone metabolism reprograms macrophages and affects CD8+ T cell responses, indicating that the tumor microenvironment can modulate this pathway. SUGCT activity is relevant to glutarate handling, and genetic variation in SUGCT modifies the severity of glutaric aciduria type 1. In bacteria and archaea, CoA-transferase expression is tuned to growth substrate, such as acetate or methylaspartate, linking enzyme levels to central carbon flux. In invertebrates, acyl-CoA transferase activity in muscle reflects energy demand and substrate supply.
CoA-transferase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| OXCT1 | Hepatocellular carcinoma progression and ketone body utilization | OXCT1 knockout or point-mutation HepG2/Huh7 cells; xenograft models |
| SUCLA2 | Liver tumor growth via OXCT1 succinylation | SUCLA2 knockout or overexpression in hepatoma cells |
| LACTB | Succinylation-dependent tumor progression | LACTB knock-in or point-mutation cells to block succinylation |
| SUGCT | Glutaric aciduria type 1 modifier | SUGCT knockout or variant knock-in patient fibroblasts |
| OXCT1 (ketolysis) | Ketone body utilization disorders | Patient-derived fibroblasts and radiolabeled acetoacetate tracing |
Hepatocellular carcinoma and OXCT1
OXCT1 functions as a succinyltransferase that succinylates LACTB, and this activity contributes to hepatocellular carcinoma progression. SUCLA2 succinylates and activates OXCT1, promoting ketolysis and liver tumor growth. Targeting OXCT1-mediated ketone metabolism reprograms macrophages to promote antitumor immunity via CD8+ T cells in hepatocellular carcinoma. Together, these studies show that CoA-transferase activity is not merely metabolic but can directly influence tumor growth and immune evasion.
Glutaric aciduria type 1 and SUGCT
Human succinyl-CoA:glutarate-CoA transferase (SUGCT) uses CoA-transferase activity to metabolize glutarate, and it is considered a putative genetic modifier of glutaric aciduria type 1. Characterization and inhibition studies of SUGCT provide a structural basis for understanding how variants in this enzyme may alter disease severity. This links GO:0008410 to an inherited neurometabolic disorder and highlights the importance of CoA-transferase chemistry in disease modification.
Ketone body utilization disorders
OXCT1 catalyzes the committing step of ketone body utilization, and loss of this activity impairs the ability of extrahepatic tissues to use ketone bodies during fasting. Radiolabeled acetoacetate has been used to trace ketone body metabolism, providing a tool to study this pathway in vivo. These findings connect CoA-transferase activity to clinical disorders of ketone body metabolism.
Microbial and invertebrate metabolism
Bacterial CoA-transferases function in the methylaspartate cycle and oxidative TCA cycle, influencing carbon assimilation and energy production. Invertebrate 2-methylbutyryl-CoA:succinate acyl-CoA transferase supports muscle energy metabolism in Ascaris suum. These non-human systems provide comparative insight into the evolution and diversity of GO:0008410.
From CoA-transferase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of OXCT1 reduce ketolysis and tumor growth? | OXCT1 knockout in hepatocellular carcinoma cell lines and xenografts |
| Does SUCLA2-mediated succinylation activate OXCT1? | SUCLA2 knockout or overexpression with OXCT1 succinylation assays |
| Does OXCT1 succinylate LACTB at specific residues? | Point-mutation knock-in of LACTB succinylation sites |
| Can SUGCT variants modify glutaric aciduria type 1? | SUGCT variant knock-in in patient-derived fibroblasts |
| Does OXCT1 modulation affect antitumor immunity? | OXCT1 knockout in tumor cells co-cultured with macrophages and CD8+ T cells |
| How is CoA-transferase activity distributed across species? | Bacterial and archaeal expression systems for mesaconate and acetate CoA-transferases |
How to Study the CoA-transferase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Coupled spectrophotometric assay | CoA-transferase activity via thioester formation | Biochemical validation of OXCT1 or SUGCT activity |
| Radiolabeled acetoacetate tracing | Ketone body utilization in vivo | Tracing ketolysis in animal models |
| 13C metabolic flux analysis | Flux through CoA-transferase-dependent pathways | Quantifying ketolysis in cancer cells |
| Anti-succinyllysine immunoblot | Protein succinylation | Detecting OXCT1 succinylation of LACTB |
| Mass spectrometry proteomics | Succinylated protein identification | Mapping succinylation targets |
| CRISPR knockout screening | Gene requirement for CoA-transferase phenotypes | Identifying modifiers of ketolysis and tumor growth |
| Co-culture immune assays | Macrophage and CD8+ T cell responses | Testing OXCT1 effects on antitumor immunity |
| Enzyme kinetics | Substrate specificity and reversibility | Comparing donor and acceptor preferences |
Enzymatic assays for CoA-transferase activity
CoA-transferase activity can be measured spectrophotometrically by coupling the production of acetoacetyl-CoA or other thioesters to NADH oxidation or by using thioester-reactive dyes. For OXCT1, assays typically use succinyl-CoA as donor and acetoacetate as acceptor and monitor acetoacetyl-CoA formation. For SUGCT, similar assays use succinyl-CoA and glutarate. These methods provide direct biochemical evidence that a candidate enzyme has GO:0008410 activity.
Metabolic tracing and flux analysis
Radiolabeled acetoacetate, such as [11C]acetoacetate, has been used to trace ketone body metabolism in vivo. Stable isotope tracing with 13C-labeled ketone bodies or succinyl-CoA can quantify flux through CoA-transferase-dependent pathways. In cancer models, tracing ketone body utilization helps determine whether OXCT1 activity supports tumor growth. These approaches connect enzyme activity to whole-cell metabolic phenotypes.
Proteomics and succinylation analysis
Because OXCT1 can act as a succinyltransferase, mass spectrometry-based proteomics can identify succinylated proteins such as LACTB. SUCLA2-dependent succinylation of OXCT1 can be detected by immunoblotting with anti-succinyllysine antibodies or by mass spectrometry. These methods link CoA-transferase activity to post-translational modification networks.
Genetic and CRISPR screens
CRISPR knockout screens can identify genes whose loss alters CoA-transferase-dependent phenotypes, such as ketolysis or tumor growth. Focused validation of OXCT1, SUCLA2, and SUGCT using knockout or knock-in models confirms causal roles. Library screening and bioinformatics can nominate additional CoA-transferase-related genes for follow-up.
How CRISPR Can Be Used to Study GO:0008410 CoA-transferase activity
Knockout
CRISPR knockout of OXCT1, SUCLA2, or SUGCT can abolish CoA-transferase activity and reveal downstream metabolic and phenotypic consequences. OXCT1 knockout in hepatocellular carcinoma cells reduces ketolysis and tumor growth, and SUCLA2 knockout prevents OXCT1 activation. SUGCT knockout models can test glutarate handling and disease modifier effects. These models provide causal evidence for GO:0008410 in disease.
Point Mutation
Point-mutation knock-in can dissect catalytic residues or regulatory sites. For example, mutating the succinylation site on OXCT1 or LACTB can test whether succinylation is required for tumor progression. Point mutations in SUGCT can model patient variants associated with glutaric aciduria type 1. These precise edits distinguish catalytic activity from scaffolding or regulatory functions.
Knock-in
Knock-in of tagged OXCT1 or SUGCT allows affinity purification and interaction studies. Tagged knock-in of OXCT1 can also enable live-cell imaging of mitochondrial localization and substrate channeling. Knock-in of disease-associated SUGCT variants into patient-derived cells provides a controlled system to study modifier effects. These models bridge biochemistry and cell biology.
Overexpression
Overexpression of OXCT1 or SUCLA2 can enhance ketolysis and succinylation, mimicking tumor-associated metabolic states. Overexpression of SUGCT can increase glutarate metabolism and test whether elevated CoA-transferase activity protects against metabolite toxicity. Overexpression models are useful for gain-of-function studies and for producing recombinant enzyme for biochemical assays.
How EDITGENE Supports CoA-transferase activity Research
Researchers studying CoA-transferase activity-related genes often need to determine whether a candidate gene is causally involved in a metabolic or disease phenotype. EDITGENE provides CRISPR-based cell model services that allow precise knockout, point mutation, knock-in, and overexpression of genes such as OXCT1, SUCLA2, SUGCT, and LACTB, enabling functional validation of GO:0008410-related hypotheses.
Contact EDITGENE today to design your custom CRISPR model for CoA-transferase activity research.
Frequently Asked Questions About CoA-transferase activity
What is CoA-transferase activity?
CoA-transferase activity (GO:0008410) is the catalysis of the transfer of a coenzyme A (CoA) group from one compound (donor) to another (acceptor), as defined by QuickGO and exemplified by enzymes such as OXCT1 and SUGCT.
What genes are involved in CoA-transferase activity?
Key human genes include OXCT1, SUCLA2, LACTB, and SUGCT, while bacterial and invertebrate examples include mesaconate CoA-transferase and 2-methylbutyryl-CoA:succinate acyl-CoA transferase.
What does OXCT1 do in ketone body metabolism?
OXCT1 catalyzes the transfer of CoA from succinyl-CoA to acetoacetate, the committing step of ketone body utilization in extrahepatic tissues.
How is CoA-transferase activity linked to cancer?
OXCT1 functions as a succinyltransferase that modifies LACTB and promotes hepatocellular carcinoma, while SUCLA2 activates OXCT1 to drive ketolysis and liver tumor growth.
What is the role of SUGCT in glutaric aciduria type 1?
SUGCT is a succinyl-CoA:glutarate-CoA transferase and a putative genetic modifier of glutaric aciduria type 1.
How can I measure CoA-transferase activity in the lab?
Coupled spectrophotometric assays, radiolabeled acetoacetate tracing, and 13C metabolic flux analysis are commonly used to measure CoA-transferase activity.
What diseases are associated with CoA-transferase dysfunction?
CoA-transferase dysfunction has been linked to hepatocellular carcinoma, glutaric aciduria type 1, and ketone body utilization disorders.
Is CoA-transferase activity found in bacteria?
Yes, bacterial CoA-transferases function in the methylaspartate cycle and oxidative TCA cycle, as shown in Haloarcula hispanica and Desulfurella acetivorans.
How do CRISPR models help study CoA-transferase activity?
CRISPR knockout, point mutation, knock-in, and overexpression models allow causal testing of genes such as OXCT1, SUCLA2, and SUGCT in metabolic and cancer phenotypes.
What is the difference between CoA-transferase and CoA ligase?
CoA-transferases move a CoA group from a donor thioester to an acceptor without ATP, whereas CoA ligases attach CoA to a carboxylate using ATP; GO:0008410 specifically describes the transfer reaction.
Conclusion
CoA-transferase activity (GO:0008410) is a conserved molecular function that moves a CoA group from a donor to an acceptor, with OXCT1 as the best-characterized human enzyme in ketone body metabolism. Beyond ketolysis, this activity contributes to protein succinylation, tumor growth, immune modulation, and inherited metabolic disease risk through enzymes such as SUGCT. Bacterial and invertebrate CoA-transferases further illustrate the broad biological and biotechnological relevance of this enzyme class. For researchers, GO:0008410 provides a precise functional annotation that can be interrogated with biochemical assays, metabolic tracing, proteomics, and CRISPR models. EDITGENE supports this work with knockout, point-mutation, knock-in, overexpression, and CRISPR screening services tailored to CoA-transferase-related genes.
References
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- 2. Guo D et al.. 2025. OXCT1 succinylation and activation by SUCLA2 promotes ketolysis and liver tumor growth.. Mol Cell 85(4):843-856.e6 PMID: 39862868
- 3. Zhu CX et al.. 2024. Targeting OXCT1-mediated ketone metabolism reprograms macrophages to promote antitumor immunity via CD8(+) T cells in hepatocellular carcinoma.. J Hepatol 81(4):690-703 PMID: 38759889
- 4. Leung K. 2004. [(11)C]Acetoacetate.. PMID: 20641818
- 5. Wu R et al.. 2024. Characterization, Structure, and Inhibition of the Human Succinyl-CoA:glutarate-CoA Transferase, a Putative Genetic Modifier of Glutaric Aciduria Type 1.. ACS Chem Biol 19(7):1544-1553 PMID: 38915184
- 6. Borjian F et al.. 2017. Succinyl-CoA:Mesaconate CoA-Transferase and Mesaconyl-CoA Hydratase, Enzymes of the Methylaspartate Cycle in Haloarcula hispanica.. Front Microbiol 8:1683 PMID: 28932214
- 7. Pettinato E et al.. 2022. Succinyl-CoA:acetate CoA-transferase functioning in the oxidative tricarboxylic acid cycle in Desulfurella acetivorans.. Front Microbiol 13:1080142 PMID: 36569052
- 8. Saz HJ et al.. 1994. 2-Methylbutyryl-CoA: succinate acyl-CoA transferase activity and function in Ascaris suum muscle.. Comp Biochem Physiol Biochem Mol Biol 108(4):513-9 PMID: 7953070
