GO:0031955 short-chain fatty acid-CoA ligase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0031955 defines short-chain fatty acid-CoA ligase activity, a molecular function that activates fatty acids with fewer than six carbons by ligating them to coenzyme A in an ATP-dependent reaction.
• The reaction consumes ATP and CoA to produce a short-chain fatty acyl-CoA, AMP, and diphosphate, a prerequisite for downstream metabolism and biosynthesis.
• Human liver mitochondria contain distinct short- and medium-chain CoA ligases that also activate xenobiotic carboxylic acids, indicating broad substrate tolerance.
• Triacsin C inhibits short-, medium-, and long-chain fatty acid:CoA ligases from human liver, making it a useful chemical probe for this activity.
• Short-chain fatty acid:CoA ligases participate in specialized biosynthetic pathways, such as branched short-chain fatty acid:CoA formation for bitter acid biosynthesis in hop glandular trichomes.
• Altered short-chain fatty acid metabolism and CoA ligase activity have been linked to metabolic phenotypes, including average daily gain divergence in beef steers and chylomicron production in enterocyte-like cells.
Description
Short-chain fatty acid-CoA ligase activity (GO:0031955) is a molecular function that catalyzes the ATP-dependent ligation of a short-chain fatty acid (fewer than six carbons) to coenzyme A, yielding a short-chain fatty acyl-CoA, AMP, and diphosphate. This activation step is essential because fatty acids must be converted to their CoA thioesters before they can enter most metabolic or biosynthetic pathways. The enzyme activity is distinct from medium- and long-chain acyl-CoA synthetases, although some enzymes can act on overlapping substrate ranges. Researchers study GO:0031955 to understand how short-chain fatty acids are channeled into energy production, lipid synthesis, and specialized metabolite pathways. In human liver mitochondria, multiple CoA ligases with activity toward short- and medium-chain fatty acids and xenobiotic carboxylic acids have been characterized, revealing the complexity of this activity in vivo. In plants, branched short-chain fatty acid:CoA ligases are involved in the biosynthesis of bitter acids in hop glandular trichomes, demonstrating the evolutionary conservation and metabolic versatility of this function. In animals, plasma carboxyl-metabolome profiles, which reflect short-chain fatty acid metabolism, have been associated with average daily gain divergence in beef steers, suggesting a role in production traits. Additionally, chylomicron production in human enterocyte-like Caco-2 cells is repressed by RPTOR knockdown, R-alpha-lipoic acid, and 4-phenylbutyric acid, linking short-chain fatty acid metabolism to lipoprotein secretion. These findings underscore the importance of GO:0031955 in basic metabolism, specialized biosynthesis, and disease-related processes.
short-chain fatty acid-CoA ligase activity At A Glance
| GO ID | GO:0031955 |
|---|---|
| GO term | short-chain fatty acid-CoA ligase activity |
| Ontology | molecular_function |
| Synonym | short-chain fatty acid activation; short-chain fatty-acid-CoA ligase activity; short-chain-fatty-acid-CoA ligase activity |
| Definition | Catalysis of the reaction: a short-chain fatty acid + ATP + CoA = a short-chain fatty acyl-CoA + AMP + diphosphate. A short-chain fatty acid has an aliphatic tail containing fewer than 6 carbons. |
| Major function | ATP-dependent activation of short-chain fatty acids by ligation to coenzyme A |
| Substrate specificity | Short-chain fatty acids with fewer than 6 carbons |
| Cofactors | ATP, CoA, Mg2+ (implied by ATP-dependent ligase mechanism) |
| Reaction products | Short-chain fatty acyl-CoA, AMP, diphosphate |
What Is GO:0031955?
GO:0031955, short-chain fatty acid-CoA ligase activity, is defined as the catalysis of the reaction: a short-chain fatty acid + ATP + CoA = a short-chain fatty acyl-CoA + AMP + diphosphate. A short-chain fatty acid has an aliphatic tail containing fewer than 6 carbons. This activity belongs to the molecular_function ontology aspect and is also known as short-chain fatty acid activation or short-chain fatty-acid-CoA ligase activity.
Why Is short-chain fatty acid-CoA ligase activity Important in Cell Biology?
GO:0031955 is important because it represents the first committed step in the metabolism of short-chain fatty acids, which are key intermediates in energy production, lipid biosynthesis, and the production of specialized metabolites. In human liver mitochondria, short-chain fatty acid:CoA ligases also activate xenobiotic carboxylic acids, suggesting a role in detoxification and drug metabolism. The activity is inhibited by triacsin C, a tool compound that has been used to dissect the contributions of different acyl-CoA ligases to cellular processes. In plants, branched short-chain fatty acid:CoA ligases are essential for bitter acid biosynthesis in hop, highlighting the agricultural and industrial relevance of this activity. In livestock, plasma carboxyl-metabolome profiles associated with average daily gain divergence in beef steers point to a role in growth and feed efficiency. In human intestinal cells, repression of chylomicron production by RPTOR knockdown and short-chain fatty acid derivatives links this activity to lipoprotein metabolism and cardiovascular risk. Thus, understanding GO:0031955 has broad implications for metabolism, pharmacology, agriculture, and disease.
• Provides activated short-chain fatty acyl-CoAs for energy production and lipid synthesis.
• Participates in the activation of xenobiotic carboxylic acids in liver mitochondria, contributing to detoxification.
• Is a target of triacsin C, a widely used inhibitor of acyl-CoA ligases, enabling functional studies.
• Supports specialized biosynthesis of bitter acids in hop glandular trichomes.
• Associates with growth and feed efficiency traits in beef cattle through plasma carboxyl-metabolome profiles.
• Links to chylomicron production and lipoprotein secretion in human enterocyte-like cells.
• May influence metabolic disorders and cardiovascular risk through short-chain fatty acid handling.
• Offers a potential target for modulating fatty acid metabolism in cancer and metabolic diseases.
• Contributes to the understanding of substrate channeling in mitochondria and peroxisomes.
• Serves as a model for studying enzyme promiscuity and substrate specificity in the CoA ligase family.
Molecular Mechanism of short-chain fatty acid-CoA ligase activity
Substrate recognition and binding
In simple terms: The enzyme grabs a short fatty acid and a CoA molecule, using ATP as an energy source.
Short-chain fatty acid-CoA ligases recognize fatty acids with aliphatic tails of fewer than six carbons. The enzyme binds the fatty acid and coenzyme A in a ternary complex with ATP. In human liver mitochondria, multiple CoA ligases with activity toward short- and medium-chain fatty acids have been isolated, indicating that substrate recognition is mediated by distinct active site pockets. The enzyme also accepts xenobiotic carboxylic acids, suggesting a relatively broad substrate tolerance.
ATP-dependent activation
In simple terms: ATP is used to activate the fatty acid, forming an intermediate that then reacts with CoA.
The catalytic mechanism involves the formation of a fatty acyl-adenylate intermediate, with the release of pyrophosphate. This step is driven by ATP hydrolysis. The activated acyl group is then transferred to the thiol group of coenzyme A, producing short-chain fatty acyl-CoA and AMP. This two-step reaction is characteristic of the ANL superfamily of adenylating enzymes, which includes acyl-CoA ligases.
Product release and channeling
In simple terms: The final product, short-chain fatty acyl-CoA, is released to be used in other metabolic pathways.
After formation, the short-chain fatty acyl-CoA is released from the enzyme. In mitochondria, these products can enter beta-oxidation, the citric acid cycle, or lipid biosynthesis. In plants, branched short-chain fatty acyl-CoAs are channeled into bitter acid biosynthesis in hop glandular trichomes. The release step may be regulated by product inhibition or by the availability of downstream enzymes.
Inhibition by triacsin C
In simple terms: A chemical called triacsin C can block this enzyme, helping researchers study its role.
Triacsin C is a potent inhibitor of short-, medium-, and long-chain fatty acid:CoA ligases from human liver. It acts as a competitive inhibitor with respect to fatty acid substrates. This compound has been widely used to probe the contribution of acyl-CoA ligases to cellular processes such as lipid synthesis and signaling. Its inhibition of short-chain fatty acid-CoA ligase activity provides a tool to dissect the specific roles of this activity in vitro and in vivo.
Regulation by cellular energy status
In simple terms: The enzyme's activity can change depending on how much energy the cell has.
Because the reaction consumes ATP, short-chain fatty acid-CoA ligase activity is sensitive to the cellular energy charge. In liver mitochondria, the activity of short- and medium-chain CoA ligases can be influenced by the availability of ATP and CoA, as well as by the redox state of the cell. Additionally, the expression of these enzymes may be regulated by metabolic hormones and nutritional status, as suggested by associations between plasma carboxyl-metabolome and growth traits in beef steers.
Key Genes Involved in GO:0031955 short-chain fatty acid-CoA ligase activity
The following genes and proteins are known to be involved in or related to short-chain fatty acid-CoA ligase activity, based on published biochemical and physiological studies.
| Gene | Major Role | Research Relevance |
|---|---|---|
| ACSM1 | Mitochondrial acyl-CoA synthetase with activity toward short- and medium-chain fatty acids | Characterized in human liver mitochondria; potential target for metabolic studies |
| ACSM2A | Mitochondrial acyl-CoA synthetase; activates short-chain fatty acids and xenobiotic carboxylic acids | Isolated from bovine liver mitochondria; used to study substrate specificity |
| ACSM2B | Mitochondrial acyl-CoA synthetase; involved in short-chain fatty acid activation | Human liver enzyme; may contribute to xenobiotic metabolism |
| ACSM3 | Acyl-CoA synthetase medium-chain family member 3; activates short-chain fatty acids | Associated with metabolic traits; potential role in energy homeostasis |
| ACSM4 | Acyl-CoA synthetase medium-chain family member 4; may activate short-chain fatty acids | Expressed in olfactory epithelium; less characterized |
| ACSM5 | Acyl-CoA synthetase medium-chain family member 5; activates short-chain fatty acids | Human liver enzyme; potential role in lipid metabolism |
| ACSS1 | Acetyl-CoA synthetase 1; activates acetate (a two-carbon short-chain fatty acid) | Mitochondrial enzyme; links to energy production |
| ACSS2 | Acetyl-CoA synthetase 2; activates acetate for lipid synthesis | Cytosolic/nuclear enzyme; important in cancer metabolism |
| ACSS3 | Acyl-CoA synthetase short-chain family member 3; activates short-chain fatty acids | Mitochondrial enzyme; function under investigation |
| HOP | Branched short-chain fatty acid:CoA ligase involved in bitter acid biosynthesis | Plant enzyme from hop glandular trichomes; studied for specialized metabolism |
| RPTOR | Regulatory-associated protein of mTOR; affects chylomicron production and short-chain fatty acid metabolism | Knockdown represses chylomicron production in Caco-2 cells |
| SLC27A2 | Fatty acid transport protein 2; may channel short-chain fatty acids to ligases | Involved in fatty acid uptake; indirect role |
| SLC27A5 | Fatty acid transport protein 5; bile acid-CoA ligase with short-chain activity | Liver-specific; links to bile acid metabolism |
| ACOT1 | Acyl-CoA thioesterase 1; hydrolyzes short-chain acyl-CoAs | Opposing activity; regulates acyl-CoA pools |
| ACOT2 | Acyl-CoA thioesterase 2; hydrolyzes short-chain acyl-CoAs | Mitochondrial; modulates fatty acid oxidation |
| CPT1A | Carnitine palmitoyltransferase 1A; uses acyl-CoAs for mitochondrial import | Downstream of ligase activity; long-chain specificity |
| PPARA | Peroxisome proliferator-activated receptor alpha; regulates lipid metabolism genes | May regulate expression of acyl-CoA ligases |
| NR1H4 | Farnesoid X receptor; regulates bile acid and lipid metabolism | Potential regulator of short-chain fatty acid-CoA ligases |
How Is short-chain fatty acid-CoA ligase activity Regulated?
Short-chain fatty acid-CoA ligase activity is regulated at multiple levels. At the transcriptional level, expression of acyl-CoA synthetase genes can be influenced by nuclear receptors such as PPARA and NR1H4, which respond to fatty acids and bile acids. At the post-transcriptional level, the activity is sensitive to cellular energy status because the reaction consumes ATP; thus, changes in ATP/AMP ratios can modulate flux through this step. Additionally, the activity can be inhibited by chemical probes such as triacsin C, which competes with fatty acid substrates. In plants, the expression of branched short-chain fatty acid:CoA ligases is developmentally regulated in glandular trichomes to support bitter acid biosynthesis. In animals, nutritional and hormonal signals may affect enzyme levels, as suggested by associations between plasma carboxyl-metabolome and average daily gain in beef steers. Furthermore, RPTOR knockdown in Caco-2 cells represses chylomicron production, indicating that mTOR signaling can influence short-chain fatty acid metabolism and lipoprotein secretion.
short-chain fatty acid-CoA ligase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| ACSM1 | Metabolic disorders, xenobiotic metabolism | Knockout in HepG2 cells; point mutation to alter substrate specificity |
| ACSM2A | Xenobiotic metabolism, liver function | Knock-in of human variant in mouse liver; overexpression in HEK293 |
| ACSM3 | Growth traits, energy homeostasis | Knockout in bovine cell lines; overexpression in adipocytes |
| ACSS2 | Cancer metabolism, lipid synthesis | Knockout in cancer cell lines; point mutation of catalytic residue |
| HOP | Bitter acid biosynthesis in hop | Knockout in hop hairy roots; overexpression in yeast |
Metabolic disorders and cardiovascular risk
Short-chain fatty acid-CoA ligase activity contributes to the activation of short-chain fatty acids, which are precursors for lipid synthesis and lipoprotein assembly. In human enterocyte-like Caco-2 cells, repression of chylomicron production by RPTOR knockdown, R-alpha-lipoic acid, and 4-phenylbutyric acid suggests that altered short-chain fatty acid metabolism can impact cardiovascular risk through changes in lipoprotein secretion. Additionally, plasma carboxyl-metabolome profiles, which reflect short-chain fatty acid handling, have been associated with average daily gain divergence in beef steers, indicating a link between this activity and metabolic efficiency.
Xenobiotic metabolism and detoxification
Human liver mitochondria contain CoA ligases that activate short- and medium-chain fatty acids as well as xenobiotic carboxylic acids. This broad substrate specificity suggests a role in the detoxification of foreign carboxylic acids by converting them to CoA thioesters, which can then be further metabolized or excreted. Deficiencies or alterations in these enzymes could affect drug metabolism and susceptibility to xenobiotic toxicity.
Cancer metabolism
Acetate, a two-carbon short-chain fatty acid, is activated by acetyl-CoA synthetases such as ACSS2 to produce acetyl-CoA, which is used for lipid synthesis and histone acetylation in cancer cells. Although ACSS2 is not specifically a short-chain fatty acid-CoA ligase per GO:0031955, its activity overlaps with the term's chemistry. Inhibitors like triacsin C, which target short-chain fatty acid:CoA ligases, have been used to study lipid metabolism in cancer. Thus, GO:0031955-related activities may contribute to cancer cell metabolism and proliferation.
Plant specialized metabolism
In hop glandular trichomes, branched short-chain fatty acid:CoA ligases are essential for the biosynthesis of bitter acids, which are important for flavor and potentially for plant defense. This highlights the agricultural and biotechnological relevance of GO:0031955 in non-human systems.
From short-chain fatty acid-CoA ligase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of ACSM1 affect short-chain fatty acid oxidation? | ACSM1 knockout in HepG2 cells |
| Can a point mutation in ACSM2A alter substrate specificity toward xenobiotics? | ACSM2A point-mutation knock-in in HEK293 cells |
| Does overexpression of ACSS2 increase acetate-dependent lipid synthesis? | ACSS2 overexpression in cancer cell lines |
| What is the effect of ACSM3 knockout on growth traits? | ACSM3 knockout in bovine myoblasts |
| Can a tagged ACSM1 knock-in reveal its subcellular localization? | Tagged ACSM1 knock-in in HeLa cells |
| Does HOP knockout reduce bitter acid production? | HOP knockout in hop glandular trichomes |
How to Study the short-chain fatty acid-CoA ligase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Spectrophotometric coupled assay | Rate of acyl-CoA formation | Enzyme kinetics and inhibitor testing |
| Radiometric assay | Incorporation of radioactive fatty acid into acyl-CoA | Substrate specificity profiling |
| LC-MS metabolomics | Levels of short-chain fatty acyl-CoAs and related metabolites | Metabolic flux analysis |
| Proteomics | Protein expression levels of acyl-CoA ligases | Tissue-specific expression studies |
| CRISPR knockout screen | Genes required for short-chain fatty acid metabolism | Functional genomics |
| Overexpression | Effect of increased enzyme levels on phenotype | Gain-of-function studies |
| Fluorescence microscopy | Subcellular localization of tagged ligases | Organelle targeting studies |
Enzymatic assays for CoA ligase activity
Short-chain fatty acid-CoA ligase activity can be measured using spectrophotometric or radiometric assays that monitor the formation of acyl-CoA from fatty acid, ATP, and CoA. For example, the release of AMP can be coupled to NADH oxidation via myokinase, pyruvate kinase, and lactate dehydrogenase, allowing continuous monitoring at 340 nm. Alternatively, radioactive substrates can be used to quantify product formation. These assays are essential for characterizing enzyme kinetics and inhibitor sensitivity, such as with triacsin C.
Proteomics and metabolomics
Comparative proteomics can identify changes in acyl-CoA ligase expression across different conditions or tissues. For instance, proteomic analysis of ovarian development in the Chinese mitten crab revealed dynamic expression of enzymes involved in fatty acid metabolism. Metabolomic profiling of plasma carboxyl-metabolome can associate short-chain fatty acid metabolism with physiological traits, as shown in beef steers. These approaches help link GO:0031955 activity to broader metabolic networks.
Cell-based models and CRISPR screens
CRISPR-Cas9 knockout screens can identify genes required for short-chain fatty acid-CoA ligase activity or for cellular processes dependent on it. For example, knocking out ACSM family genes in liver cell lines followed by lipidomics can reveal their contributions to lipid metabolism. Overexpression or point-mutation knock-in models can test the effect of specific amino acid changes on substrate specificity. These models are complemented by RNA-seq to measure transcriptional responses.
Imaging and subcellular localization
Fluorescent tagging of acyl-CoA ligases (e.g., GFP fusion) can reveal their subcellular localization in mitochondria, peroxisomes, or cytosol. This is important because short-chain fatty acid-CoA ligases are found in different compartments, and their localization affects substrate access. Live-cell imaging can also track the dynamics of lipid droplets or acyl-CoA pools using fluorescent reporters.
How CRISPR Can Be Used to Study GO:0031955 short-chain fatty acid-CoA ligase activity
Knockout
CRISPR-Cas9 knockout of genes encoding short-chain fatty acid-CoA ligases (e.g., ACSM1, ACSM2A) can abolish or reduce enzymatic activity, allowing researchers to study the consequences for fatty acid metabolism, energy production, and xenobiotic detoxification. For example, knockout of ACSM1 in HepG2 cells can reveal its role in mitochondrial short-chain fatty acid oxidation. Knockout models are also useful for validating inhibitor specificity, such as triacsin C.
Point Mutation
Point mutations can be introduced into the active site of short-chain fatty acid-CoA ligases to alter substrate specificity or catalytic efficiency. For instance, mutating the conserved lysine residue involved in ATP binding can create an inactive enzyme, serving as a negative control. Alternatively, mutations that broaden substrate specificity toward longer-chain fatty acids can help map the determinants of chain-length selectivity.
Knock-in
Knock-in of tagged versions (e.g., FLAG, GFP) of short-chain fatty acid-CoA ligases allows for affinity purification and localization studies. Knock-in of disease-associated variants can model human metabolic disorders. For example, knocking in a human ACSM2A variant into mouse liver can test its effect on xenobiotic metabolism.
Overexpression
Overexpression of short-chain fatty acid-CoA ligases in cell lines (e.g., HEK293, Caco-2) can increase flux through short-chain fatty acid activation pathways, leading to elevated acyl-CoA levels and altered lipid metabolism. This approach is useful for studying downstream effects on chylomicron production, as shown with RPTOR knockdown and 4-phenylbutyric acid treatment in Caco-2 cells. Overexpression can also sensitize cells to triacsin C inhibition.
How EDITGENE Supports short-chain fatty acid-CoA ligase activity Research
Researchers studying short-chain fatty acid-CoA ligase activity-related genes often need to determine whether a candidate gene is causally involved in a specific metabolic or disease phenotype. This requires precise genetic models that can knockout, mutate, tag, or overexpress the gene of interest in relevant cell types. EDITGENE provides a comprehensive suite of CRISPR-based services to accelerate such investigations, from single-gene editing to high-throughput library screening.
Contact EDITGENE today to design your custom CRISPR model for short-chain fatty acid-CoA ligase activity research.
Frequently Asked Questions About short-chain fatty acid-CoA ligase activity
What is short-chain fatty acid-CoA ligase activity?
Short-chain fatty acid-CoA ligase activity (GO:0031955) is a molecular function that catalyzes the ATP-dependent ligation of a short-chain fatty acid (fewer than six carbons) to coenzyme A, producing a short-chain fatty acyl-CoA, AMP, and diphosphate.
What genes are involved in short-chain fatty acid-CoA ligase activity?
Genes encoding enzymes with this activity include ACSM1, ACSM2A, ACSM2B, ACSM3, ACSM4, ACSM5, ACSS1, ACSS2, and ACSS3 in humans, as well as HOP in plants.
What is the reaction catalyzed by GO:0031955?
The reaction is: a short-chain fatty acid + ATP + CoA = a short-chain fatty acyl-CoA + AMP + diphosphate. A short-chain fatty acid has an aliphatic tail containing fewer than 6 carbons.
How is short-chain fatty acid-CoA ligase activity regulated?
It is regulated by cellular energy status (ATP/AMP ratio), transcriptional control via nuclear receptors such as PPARA, and can be inhibited by chemical probes like triacsin C.
What diseases are associated with short-chain fatty acid-CoA ligase activity?
Altered activity has been linked to metabolic disorders, cardiovascular risk through chylomicron production, xenobiotic toxicity, and cancer metabolism.
What is the difference between short-chain and long-chain fatty acid-CoA ligases?
Short-chain fatty acid-CoA ligases act on fatty acids with fewer than 6 carbons, while long-chain acyl-CoA synthetases act on fatty acids with 12 or more carbons. Medium-chain enzymes act on 6-12 carbons. Triacsin C inhibits all three classes.
Can triacsin C inhibit short-chain fatty acid-CoA ligase activity?
Yes, triacsin C is a potent inhibitor of short-, medium-, and long-chain fatty acid:CoA ligases from human liver, making it a useful tool for studying this activity.
What model systems are used to study short-chain fatty acid-CoA ligase activity?
Common models include human liver mitochondria, HepG2 and Caco-2 cell lines, bovine liver mitochondria, hop glandular trichomes, and CRISPR knockout or overexpression cell lines.
How can I measure short-chain fatty acid-CoA ligase activity in the lab?
Activity can be measured using coupled spectrophotometric assays that monitor AMP release or radiometric assays with labeled fatty acids. LC-MS can quantify acyl-CoA products.
What CRISPR services does EDITGENE offer for studying this activity?
EDITGENE provides knockout, point mutation, knock-in, tagged knock-in, overexpression cell models, CRISPR library screening, and bioinformatics support for genes related to short-chain fatty acid-CoA ligase activity.
Conclusion
Short-chain fatty acid-CoA ligase activity (GO:0031955) is a fundamental molecular function that activates short-chain fatty acids for diverse metabolic and biosynthetic pathways. Its roles range from mitochondrial energy production and xenobiotic detoxification in humans to bitter acid biosynthesis in plants. Dysregulation of this activity has been linked to metabolic disorders, cardiovascular risk, and cancer metabolism. Understanding its mechanism, regulation, and genetic determinants requires robust experimental models. EDITGENE's CRISPR services provide the tools needed to dissect this activity and its associated genes in health and disease.
References
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- 2. Xu H et al.. 2013. Characterization of the formation of branched short-chain fatty acid:CoAs for bitter acid biosynthesis in hop glandular trichomes.. Mol Plant 6(4):1301-17 PMID: 23300257
- 3. Vessey DA et al.. 1999. Characterization of the CoA ligases of human liver mitochondria catalyzing the activation of short- and medium-chain fatty acids and xenobiotic carboxylic acids.. Biochim Biophys Acta 1428(2-3):455-62 PMID: 10434065
- 4. Vanden Heuvel JP et al.. 1991. Inhibition of long-chain acyl-CoA synthetase by the peroxisome proliferator perfluorodecanoic acid in rat hepatocytes.. Biochem Pharmacol 42(2):295-302 PMID: 1859447
- 5. Ogunade I et al.. 2021. Plasma Carboxyl-Metabolome Is Associated with Average Daily Gain Divergence in Beef Steers.. Animals (Basel) 11(1) PMID: 33401431
- 6. He B et al.. 2022. Chylomicron production is repressed by RPTOR knockdown, R-α-lipoic acid and 4-phenylbutyric acid in human enterocyte-like Caco-2 cells.. J Nutr Biochem 108:109087 PMID: 35691593
- 7. Vessey DA et al.. 1995. Isolation from bovine liver mitochondria and characterization of three distinct carboxylic acid: CoA ligases with activity toward xenobiotics.. J Biochem Toxicol 10(6):329-37 PMID: 8934636
- 8. Feng QM et al.. 2021. Comparative proteomics elucidates the dynamics of ovarian development in the Chinese mitten crab Eriocheir sinensis.. Comp Biochem Physiol Part D Genomics Proteomics 40:100878 PMID: 34333232
