GO:0004092 carnitine O-acetyltransferase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0004092 carnitine O-acetyltransferase activity catalyzes the reversible transfer of an acetyl group between acetyl-CoA and carnitine, producing (R)-O-acetylcarnitine and CoA.
• The enzyme is central to lipid and branched-chain amino acid metabolism, epigenetics, cell plasticity, and organelle function.
• CRAT activity is reduced in Alzheimer's disease brain microvessels and is inhibited by bile acids, linking it to neurodegeneration and metabolic dysfunction.
• Obesity and lipid stress inhibit carnitine acetyltransferase activity, and skeletal muscle mitochondrial inertia is associated with CRAT activity and physical function in humans.
• The p.Tyr110Cys CRAT variant is associated with an early-onset case of Leigh syndrome, and modulators of this variant have been identified through combined in silico/in vitro approaches.
• Heterocyclic gamma-butyrobetaines have been rationally designed and synthesized as potential carnitine acetyltransferase inhibitors.
Description
Carnitine O-acetyltransferase activity (GO:0004092) is a molecular function defined by the catalysis of the reaction acetyl-CoA + carnitine = (R)-O-acetylcarnitine + CoA. This reversible acetyl-transfer reaction sits at the intersection of acyl-CoA metabolism and carnitine homeostasis, enabling cells to buffer and shuttle acetyl units between mitochondrial and cytosolic compartments. The enzyme responsible for this activity, commonly known as carnitine acetyltransferase (CRAT), is a member of the carnitine acyltransferase family and is widely distributed across tissues, with particularly high activity in tissues that rely on fatty acid oxidation and acetyl-CoA flux, such as skeletal muscle, heart, and liver. Because the reaction directly consumes acetyl-CoA and generates acetylcarnitine, it influences the availability of acetyl-CoA for the tricarboxylic acid cycle, ketogenesis, and protein acetylation reactions. Consequently, researchers studying mitochondrial metabolism, metabolic flexibility, and epigenetic regulation frequently encounter GO:0004092 as a key node in their experimental systems. The clinical relevance of this activity is underscored by its reduced levels in Alzheimer's disease brain microvessels and its inhibition by bile acids, as well as by the identification of a CRAT variant associated with Leigh syndrome.
carnitine O-acetyltransferase activity At A Glance
| GO ID | GO:0004092 |
|---|---|
| GO term | carnitine O-acetyltransferase activity |
| Ontology | molecular_function |
| Synonym | acetylcarnitine transferase activity; acetyl-CoA-carnitine O-acetyltransferase activity; carnitine acetylase activity; carnitine acetyltransferase activity; CATC |
| Major function | Catalysis of the reversible transfer of an acetyl group between acetyl-CoA and carnitine, yielding (R)-O-acetylcarnitine and CoA |
| Reaction | acetyl-CoA + carnitine = (R)-O-acetylcarnitine + CoA |
| Subcellular context | Associated with mitochondrial and peroxisomal compartments, influencing acetyl-CoA buffering and organelle function |
| Physiological role | Central player in lipid and branched-chain amino acid metabolism, epigenetics, cell plasticity, and organelle function |
| Disease relevance | Reduced activity in Alzheimer's disease brain microvessels; inhibition by bile acids; CRAT variant linked to Leigh syndrome |
What Is GO:0004092?
In simple terms, carnitine O-acetyltransferase activity is the ability of an enzyme to move an acetyl group from acetyl-CoA onto carnitine, forming acetylcarnitine and free CoA, and to reverse this reaction. The QuickGO definition states that this activity catalyzes the reaction: acetyl-CoA + carnitine = (R)-O-acetylcarnitine + CoA. This reaction is reversible and does not consume ATP, distinguishing it from the carnitine palmitoyltransferase reactions involved in fatty acid import. The activity is classified as a molecular_function in the Gene Ontology and is synonymous with terms such as acetylcarnitine transferase activity, carnitine acetylase activity, and CATC.
Why Is carnitine O-acetyltransferase activity Important in Cell Biology?
Carnitine O-acetyltransferase activity is important because it directly modulates the cellular pools of acetyl-CoA and acetylcarnitine, two metabolites that influence energy production, metabolic signaling, and protein acetylation. By reversibly converting acetyl-CoA to acetylcarnitine, the enzyme acts as a buffer for acetyl groups, allowing tissues to maintain acetyl-CoA homeostasis during fluctuations in fatty acid oxidation and glucose metabolism. This buffering capacity is particularly relevant in skeletal muscle, where carnitine acetyltransferase activity is associated with mitochondrial inertia and physical function in humans. Moreover, the activity is sensitive to metabolic stress: obesity and lipid stress inhibit carnitine acetyltransferase activity, suggesting a link between nutrient overload and impaired acetyl handling. In the brain, decreased carnitine acetyltransferase activity in microvessels has been reported in Alzheimer's disease, pointing to a possible role in neurovascular dysfunction. The identification of a CRAT variant associated with Leigh syndrome further highlights the clinical importance of this activity for mitochondrial energy metabolism.
• Buffers acetyl-CoA pools, supporting mitochondrial energy metabolism and metabolic flexibility.
• Links lipid metabolism and branched-chain amino acid metabolism to epigenetic regulation and cell plasticity.
• Supports skeletal muscle mitochondrial function and physical performance in humans.
• Is inhibited by obesity and lipid stress, contributing to metabolic dysfunction.
• Is decreased in Alzheimer's disease brain microvessels, suggesting a role in neurodegeneration.
• Is inhibited by bile acids, which has implications for carnitine analysis and liver metabolism.
• A CRAT variant (p.Tyr110Cys) is associated with early-onset Leigh syndrome, a severe mitochondrial disorder.
• Represents a potential target for small-molecule modulators, including heterocyclic gamma-butyrobetaines.
• Influences organelle function, including mitochondrial and peroxisomal acetyl-CoA handling.
• Provides a mechanistic node for understanding metabolic reprogramming in disease states.
What Happens During carnitine O-acetyltransferase activity?
Substrate binding and acetyl transfer
In simple terms: The enzyme grabs an acetyl group from acetyl-CoA and hands it to carnitine.
The catalytic cycle begins with the binding of acetyl-CoA and carnitine to the enzyme's active site. Carnitine O-acetyltransferase catalyzes the reversible transfer of the acetyl moiety from acetyl-CoA to carnitine, producing (R)-O-acetylcarnitine and free CoA. This reaction does not require ATP and proceeds via a ping-pong or sequential mechanism typical of acyltransferases, although the exact kinetic order may vary among isoforms. The reaction is readily reversible, allowing the enzyme to regenerate acetyl-CoA from acetylcarnitine when needed.
Acetylcarnitine formation and acetyl-CoA buffering
In simple terms: The enzyme converts excess acetyl-CoA into acetylcarnitine, which acts as a storage form of acetyl groups.
By forming acetylcarnitine, carnitine O-acetyltransferase activity provides a sink for acetyl groups when acetyl-CoA production exceeds the capacity of the tricarboxylic acid cycle or other acetyl-CoA-consuming pathways. This buffering role is particularly important in tissues with high fatty acid oxidation rates, such as skeletal muscle and heart, where acetylcarnitine can accumulate and later be converted back to acetyl-CoA. The reversible nature of the reaction allows the enzyme to respond dynamically to changes in substrate availability and energy demand.
Compartmental shuttling of acetyl units
In simple terms: The enzyme helps move acetyl groups between different parts of the cell.
Carnitine O-acetyltransferase activity is present in mitochondria and peroxisomes, where it contributes to the exchange of acetyl units across organelle membranes. By converting acetyl-CoA to acetylcarnitine, the enzyme enables acetyl groups to traverse membranes that are impermeable to CoA derivatives, facilitating the transfer of acetyl units from sites of production to sites of utilization. This shuttling function is essential for maintaining metabolic coordination between organelles and the cytosol.
Integration with branched-chain amino acid metabolism
In simple terms: The enzyme also participates in processing byproducts of branched-chain amino acid breakdown.
Carnitine O-acetyltransferase activity is linked to branched-chain amino acid metabolism, as acetyl-CoA and related acyl-CoAs generated from these amino acids can be substrates for the enzyme. This integration allows the enzyme to contribute to the clearance of acyl groups derived from multiple nutrient sources, connecting lipid and amino acid catabolism. Dysregulation of this integration may contribute to metabolic disorders characterized by acyl-CoA accumulation.
Regulation by substrate availability and inhibitors
In simple terms: The enzyme's speed depends on how much substrate is around and can be slowed by certain molecules.
The activity of carnitine O-acetyltransferase is influenced by the availability of acetyl-CoA and carnitine, as well as by the acetylcarnitine/CoA ratio. In addition, bile acids have been shown to inhibit carnitine acetyltransferase, which can affect carnitine analysis and may have physiological implications in cholestatic conditions. Obesity and lipid stress also inhibit carnitine acetyltransferase activity, suggesting that nutrient overload can directly suppress this function. These regulatory inputs position the enzyme as a metabolic sensor that responds to both substrate supply and pathological stressors.
Key Genes Involved in GO:0004092 carnitine O-acetyltransferase activity
The following genes and proteins are directly or indirectly associated with carnitine O-acetyltransferase activity, based on published literature.
| Gene | Major Role | Research Relevance |
|---|---|---|
| CRAT | Encodes carnitine O-acetyltransferase, the enzyme responsible for GO:0004092 activity | Central to studies of acetyl-CoA buffering, metabolic flexibility, and Leigh syndrome |
| ACAT1 | Mitochondrial acetoacetyl-CoA thiolase, involved in ketone body metabolism and acetyl-CoA flux | May influence substrate availability for CRAT |
| CPT1A | Carnitine palmitoyltransferase 1A, controls fatty acid entry into mitochondria | Provides acyl-CoA substrates that can feed into acetyl-CoA pools |
| CPT2 | Carnitine palmitoyltransferase 2, involved in fatty acid oxidation | Linked to mitochondrial acyl-CoA metabolism and carnitine shuttle |
| SLC25A20 | Carnitine-acylcarnitine translocase, transports acylcarnitines across inner mitochondrial membrane | Affects carnitine and acetylcarnitine transport |
| BCKDHA | Branched-chain alpha-keto acid dehydrogenase E1 alpha, involved in BCAA catabolism | Connects BCAA metabolism to acetyl-CoA and CRAT activity |
| BCKDHB | Branched-chain alpha-keto acid dehydrogenase E1 beta | Contributes to acetyl-CoA production from BCAA |
| DBT | Dihydrolipoamide branched chain transacylase E2 | Part of BCAA dehydrogenase complex feeding acetyl-CoA |
| DLD | Dihydrolipoamide dehydrogenase, shared component of dehydrogenase complexes | Supports acetyl-CoA generation from multiple sources |
| ACACA | Acetyl-CoA carboxylase alpha, consumes acetyl-CoA for fatty acid synthesis | Competes with CRAT for acetyl-CoA |
| ACACB | Acetyl-CoA carboxylase beta, regulates fatty acid oxidation | Influences acetyl-CoA availability for CRAT |
| HAT1 | Histone acetyltransferase, uses acetyl-CoA for histone acetylation | Links CRAT-mediated acetyl-CoA buffering to epigenetics |
| EP300 | Histone acetyltransferase p300, acetylates histones and non-histone proteins | Epigenetic reader of acetyl-CoA pools influenced by CRAT |
| CREBBP | CREB-binding protein, acetyltransferase | Connects acetyl-CoA metabolism to transcriptional regulation |
| SIRT1 | NAD-dependent deacetylase, responds to metabolic state | May interact with acetyl-CoA and acetylcarnitine levels |
| SIRT3 | Mitochondrial deacetylase, regulates metabolic enzymes | Potential link between CRAT activity and mitochondrial acetylation |
| PPARGC1A | PGC-1alpha, master regulator of mitochondrial biogenesis | May influence CRAT expression and mitochondrial function |
How Is carnitine O-acetyltransferase activity Regulated?
Carnitine O-acetyltransferase activity is regulated at multiple levels. Substrate availability of acetyl-CoA and carnitine directly determines flux through the reaction, and the acetylcarnitine/CoA ratio can shift the equilibrium. In addition, the activity is inhibited by bile acids, which may be relevant in cholestatic liver disease and in analytical settings where bile acids interfere with carnitine measurements. Obesity and lipid stress have been shown to inhibit carnitine acetyltransferase activity, suggesting that nutrient overload and inflammatory signals can suppress the enzyme. At the transcriptional level, the CRAT gene may be influenced by metabolic transcription factors such as PGC-1alpha, which coordinates mitochondrial biogenesis and metabolic gene expression. Post-translational modifications, including acetylation and phosphorylation, could also modulate CRAT activity, although specific sites and mechanisms require further investigation. Overall, the regulation of GO:0004092 ensures that acetyl group buffering is matched to the metabolic state of the cell.
carnitine O-acetyltransferase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| CRAT | Leigh syndrome (p.Tyr110Cys variant) | Patient-derived fibroblasts or induced pluripotent stem cells with CRISPR-corrected variant |
| CRAT | Alzheimer's disease (reduced brain microvessel activity) | CRAT knockout or knockdown in brain endothelial cell lines |
| CRAT | Obesity and lipid stress (inhibited activity) | High-fat diet mouse models with CRAT overexpression or knockout |
| CRAT | Skeletal muscle mitochondrial inertia | CRAT knockout in C2C12 myotubes or primary human myotubes |
| CRAT | Bile acid inhibition | Hepatocyte cell lines treated with bile acids and CRAT inhibitors |
Leigh syndrome and mitochondrial disease
A homozygous or compound heterozygous variant in CRAT, p.Tyr110Cys, has been associated with an early-onset case of Leigh syndrome, a severe mitochondrial disorder characterized by neurodegeneration and metabolic decompensation. Functional studies using combined in silico and in vitro approaches have identified small-molecule modulators that can influence the activity of this variant, providing a potential therapeutic avenue. This case highlights the critical role of carnitine O-acetyltransferase activity in mitochondrial energy metabolism and the consequences of its dysfunction.
Alzheimer's disease and neurodegeneration
Carnitine acetyltransferase activity is decreased in human brain microvessels in Alzheimer's disease compared to controls, suggesting that impaired acetyl buffering may contribute to neurovascular dysfunction. The reduction in activity could affect acetyl-CoA availability for acetylcholine synthesis and other neuronal functions, although the exact mechanisms remain to be fully elucidated. This finding positions GO:0004092 as a potential biomarker or therapeutic target in neurodegenerative conditions.
Obesity, lipid stress, and metabolic dysfunction
Obesity and lipid stress inhibit carnitine acetyltransferase activity, as demonstrated in experimental models. This inhibition may contribute to impaired metabolic flexibility and acetyl-CoA accumulation, which are hallmarks of insulin resistance and type 2 diabetes. In skeletal muscle, mitochondrial inertia is associated with carnitine acetyltransferase activity and physical function in humans, indicating that reduced CRAT activity may underlie exercise intolerance in metabolic disease. These observations link GO:0004092 to the pathophysiology of obesity and related disorders.
Liver disease and bile acid effects
Bile acids inhibit carnitine acetyltransferase, which has implications for carnitine analysis and potentially for liver metabolism in cholestatic conditions. The inhibition may alter hepatic acetyl-CoA and acetylcarnitine levels, affecting energy homeostasis and detoxification pathways. Further research is needed to determine whether this inhibition contributes to liver injury in diseases such as primary biliary cholangitis.
From carnitine O-acetyltransferase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| What is the effect of CRAT loss on acetyl-CoA and acetylcarnitine levels? | CRAT knockout cell lines (e.g., HEK293T, HepG2) generated by CRISPR |
| Does the p.Tyr110Cys CRAT variant alter enzyme kinetics? | Point-mutation knock-in cell lines expressing the variant |
| Can a tagged CRAT be used to study subcellular localization? | Knock-in of fluorescent or affinity tags at the endogenous CRAT locus |
| Does CRAT overexpression protect against lipid stress? | CRAT overexpression in skeletal muscle cells or mouse models |
| What is the impact of CRAT on mitochondrial function? | CRAT knockout in primary myotubes or cardiomyocytes |
| Can small molecules modulate CRAT activity? | In vitro enzymatic assays with recombinant CRAT and candidate inhibitors |
How to Study the carnitine O-acetyltransferase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Spectrophotometric activity assay | Carnitine O-acetyltransferase enzymatic activity | Characterization of wild-type and mutant CRAT |
| LC-MS metabolomics | Acetylcarnitine, acetyl-CoA, and related metabolites | Metabolic profiling of cells with CRAT knockout or overexpression |
| CRISPR knockout | Loss-of-function effects on acetyl-CoA metabolism | Studying metabolic flexibility and mitochondrial function |
| CRISPR point mutation | Effect of specific CRAT variants on activity | Modeling Leigh syndrome-associated p.Tyr110Cys variant |
| Tagged knock-in | Subcellular localization and protein interactions | Live-cell imaging and proteomics of CRAT |
| CRISPR library screening | Genes that modulate CRAT activity or synthetic lethality | Identifying metabolic vulnerabilities |
| RNA-seq | Transcriptional changes upon CRAT manipulation | Pathway analysis of acetyl-CoA-related genes |
| Proteomics | Protein acetylation and expression changes | Linking CRAT activity to epigenetic and signaling networks |
Enzymatic activity assays
Carnitine O-acetyltransferase activity can be measured using spectrophotometric or radiometric assays that monitor the formation of acetylcarnitine or CoA. These assays typically use acetyl-CoA and carnitine as substrates and detect the release of CoA using thiol-reactive reagents such as DTNB. Such methods are essential for characterizing wild-type and mutant CRAT variants, including the p.Tyr110Cys variant associated with Leigh syndrome.
Metabolomics and acetylcarnitine quantification
Mass spectrometry-based metabolomics allows quantification of acetylcarnitine, acetyl-CoA, and related metabolites in cells and tissues. These approaches can reveal how changes in CRAT activity affect acetyl-CoA buffering and metabolic flux. Targeted methods using stable isotope-labeled internal standards provide accurate measurements of carnitine and acylcarnitine species.
Genetic manipulation and CRISPR screens
CRISPR-Cas9 knockout, point mutation, and knock-in strategies enable precise interrogation of CRAT function in cellular models. Pooled CRISPR screens can identify genes that modulate carnitine O-acetyltransferase activity or that are synthetically lethal with CRAT loss. Such screens are powerful for uncovering genetic interactions and pathways that buffer acetyl-CoA metabolism.
Protein interaction and localization studies
Immunoprecipitation, proximity labeling, and fluorescence microscopy can be used to study CRAT protein interactions and subcellular localization. Tagged knock-in cell lines expressing CRAT with fluorescent or affinity tags allow live-cell imaging and proteomic analysis. These methods help define the organelle-specific roles of carnitine O-acetyltransferase activity.
How CRISPR Can Be Used to Study GO:0004092 carnitine O-acetyltransferase activity
Knockout
CRISPR-Cas9 knockout of CRAT eliminates carnitine O-acetyltransferase activity, allowing researchers to study the consequences of losing acetyl-CoA buffering. CRAT knockout cells often show altered acetylcarnitine levels, reduced metabolic flexibility, and changes in mitochondrial function. These models are valuable for dissecting the role of GO:0004092 in lipid and branched-chain amino acid metabolism.
Point Mutation
CRISPR-mediated point mutation can introduce specific disease-associated variants, such as the p.Tyr110Cys CRAT variant linked to Leigh syndrome. These models enable precise evaluation of how a single amino acid change affects enzyme kinetics, substrate affinity, and cellular metabolism. They are also useful for testing small-molecule modulators that may rescue mutant activity.
Knock-in
Knock-in of tags or reporter genes at the endogenous CRAT locus allows real-time monitoring of protein expression, localization, and interactions. Fluorescent tags enable live-cell imaging of CRAT in mitochondria and peroxisomes, while affinity tags facilitate proteomic identification of interacting partners. Such models provide insights into the spatiotemporal regulation of carnitine O-acetyltransferase activity.
Overexpression
CRISPR activation or lentiviral overexpression of CRAT can increase carnitine O-acetyltransferase activity, allowing researchers to test whether enhanced acetyl buffering protects against metabolic stress. Overexpression models are useful for studying the effects of increased acetylcarnitine production on mitochondrial function and cell survival. They can also be used to screen for substrates or inhibitors that interact with the enzyme.
How EDITGENE Supports carnitine O-acetyltransferase activity Research
Researchers studying carnitine O-acetyltransferase activity-related genes often need to determine whether a candidate gene is causally involved in metabolic phenotypes, disease susceptibility, or drug response. EDITGENE provides a comprehensive suite of CRISPR-based services to generate precisely engineered cell models, enabling rigorous functional validation of genes linked to GO:0004092.
Contact EDITGENE today to design your custom CRISPR model for carnitine O-acetyltransferase activity research.
Frequently Asked Questions About carnitine O-acetyltransferase activity
What is carnitine O-acetyltransferase activity?
Carnitine O-acetyltransferase activity (GO:0004092) is a molecular function that catalyzes the reversible transfer of an acetyl group from acetyl-CoA to carnitine, forming (R)-O-acetylcarnitine and CoA.
What genes are involved in carnitine O-acetyltransferase activity?
The primary gene is CRAT, which encodes the enzyme carnitine O-acetyltransferase. Other genes such as CPT1A, CPT2, and SLC25A20 influence related carnitine and acyl-CoA metabolism.
What is the role of CRAT in metabolism?
CRAT buffers acetyl-CoA pools by converting acetyl-CoA to acetylcarnitine, supporting mitochondrial energy metabolism, metabolic flexibility, and integration of lipid and branched-chain amino acid catabolism.
How is carnitine O-acetyltransferase activity measured?
It is typically measured using spectrophotometric or radiometric assays that detect the formation of CoA or acetylcarnitine, often with DTNB or radiolabeled substrates.
What diseases are associated with carnitine O-acetyltransferase deficiency?
CRAT variants, such as p.Tyr110Cys, have been linked to Leigh syndrome. Reduced activity is also observed in Alzheimer's disease brain microvessels and in obesity-related metabolic dysfunction.
Is carnitine O-acetyltransferase activity inhibited by bile acids?
Yes, bile acids have been shown to inhibit carnitine acetyltransferase, which can interfere with carnitine analysis and may have implications for liver disease.
Can carnitine O-acetyltransferase activity be targeted by drugs?
Yes, heterocyclic gamma-butyrobetaines have been designed and synthesized as potential inhibitors of carnitine acetyltransferase, and modulators of the p.Tyr110Cys variant have been identified.
What is the difference between CRAT and CPT1?
CRAT catalyzes the reversible acetylation of carnitine using acetyl-CoA, while CPT1 catalyzes the transfer of long-chain acyl groups from acyl-CoA to carnitine for mitochondrial fatty acid import.
How does obesity affect carnitine acetyltransferase activity?
Obesity and lipid stress inhibit carnitine acetyltransferase activity, which may contribute to impaired metabolic flexibility and acetyl-CoA accumulation.
What model systems are used to study carnitine O-acetyltransferase activity?
Common models include CRAT knockout and knock-in cell lines, patient-derived fibroblasts, and animal models of metabolic disease, often combined with CRISPR editing and metabolomics.
Conclusion
Carnitine O-acetyltransferase activity (GO:0004092) is a fundamental molecular function that governs acetyl-CoA buffering and acetylcarnitine production, with far-reaching implications for lipid metabolism, branched-chain amino acid catabolism, epigenetics, and organelle function. Its dysfunction is linked to severe mitochondrial disorders such as Leigh syndrome, as well as to neurodegenerative and metabolic diseases. Continued research using CRISPR-based models and advanced metabolomics will further illuminate the mechanistic roles of this activity and may uncover therapeutic strategies for associated conditions.
References
- 1. Volpicella M et al.. 2025. Carnitine O-Acetyltransferase as a Central Player in Lipid and Branched-Chain Amino Acid Metabolism, Epigenetics, Cell Plasticity, and Organelle Function.. Biomolecules 15(2) PMID: 40001519
- 2. Cafferati Beltrame L et al.. 2025. Combined in silico/in vitro approaches for identifying modulators of the activity of the p.Tyr110Cys Carnitine O-Acetyltransferase (CRAT) variant associated to an early onset case of Leigh syndrome.. Acta Pharmacol Sin 46(4):1123-1136 PMID: 39681600
- 3. Bremer J. 1983. Carnitine--metabolism and functions.. Physiol Rev 63(4):1420-80 PMID: 6361812
- 4. Mancilla RF et al.. 2023. Skeletal muscle mitochondrial inertia is associated with carnitine acetyltransferase activity and physical function in humans.. JCI Insight 8(1) PMID: 36413408
- 5. Seiler SE et al.. 2014. Obesity and lipid stress inhibit carnitine acetyltransferase activity.. J Lipid Res 55(4):635-44 PMID: 24395925
- 6. Stoyanova S et al.. 2025. Rational Design, Synthesis, and In Vitro Activity of Heterocyclic Gamma-Butyrobetaines as Potential Carnitine Acetyltransferase Inhibitors.. Molecules 30(3) PMID: 39942839
- 7. Kalaria RN et al.. 1992. Carnitine acetyltransferase activity in the human brain and its microvessels is decreased in Alzheimer's disease.. Ann Neurol 32(4):583-6 PMID: 1456745
- 8. Sekas G et al.. 1989. Inhibition of carnitine acetyltransferase by bile acids: implications for carnitine analysis.. Anal Biochem 179(2):262-7 PMID: 2774175
