GO:0120573 FAHFA hydrolase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0120573 (FAHFA hydrolase activity) is a molecular function that catalyzes hydrolysis of the ester bond in fatty acid esters of hydroxy fatty acids (FAHFAs), releasing a free fatty acid and a hydroxy fatty acid.
• FAHFAs are endogenous bioactive signaling lipids, and their levels are controlled by the balance between biosynthesis and hydrolysis.
• AIG1 and ADTRP are the principal endogenous FAHFA hydrolases identified in mice, and they are members of the serine hydrolase superfamily.
• ATGL (PNPLA2) acts as a biosynthetic enzyme for FAHFAs, opposing the hydrolytic activity of AIG1 and ADTRP.
• FAHFA metabolism is dynamically regulated by fasting, acute inflammation, and diet-induced obesity, linking GO:0120573 to metabolic disease.
• Studying GO:0120573 requires combining lipidomics, activity-based protein profiling, and CRISPR-based genetic models.
Description
FAHFA hydrolase activity (GO:0120573) is the molecular function that catalyzes the hydrolysis of the ester bond in a fatty acid ester of a hydroxy fatty acid (FAHFA), yielding a free fatty acid and a hydroxy fatty acid. FAHFAs are a class of endogenous bioactive signaling lipids in which a fatty acid is esterified to a hydroxyl group on a second fatty acid backbone, and they have attracted attention for their roles in insulin sensitivity, inflammation, and energy metabolism. The discovery that AIG1 and ADTRP function as endogenous FAHFA hydrolases established that FAHFA levels are actively controlled by dedicated hydrolytic enzymes rather than by passive chemical hydrolysis alone. This finding made GO:0120573 a focal point for understanding how cells set the steady-state concentration of these signaling lipids. From a research perspective, GO:0120573 matters because it provides a direct enzymatic counterweight to FAHFA biosynthesis. ATGL (PNPLA2) was identified as a biosynthetic enzyme for FAHFAs, and its activity increases FAHFA levels in white adipose tissue during fasting. Conversely, AIG1 and ADTRP hydrolyze FAHFAs and thereby lower their abundance. The interplay between these opposing activities determines the pool of bioactive FAHFAs available for receptor-mediated signaling and metabolic regulation. Because FAHFA levels change in obesity, inflammation, and fasting, the enzymes that execute GO:0120573 are candidate therapeutic targets and biomarkers. Finally, GO:0120573 is experimentally tractable. Activity-based probes such as fluorophosphonate-alkyne reagents label serine hydrolases and enable profiling of FAHFA hydrolase candidates in native proteomes. Combined with CRISPR knockout, point mutation, and overexpression models, these tools allow researchers to assign hydrolase activity to specific gene products and to test causality in metabolic phenotypes. This article summarizes the definition, mechanism, key genes, disease links, and research methods for GO:0120573.
FAHFA hydrolase activity At A Glance
| GO ID | GO:0120573 |
|---|---|
| GO term | FAHFA hydrolase activity |
| Ontology | molecular_function |
| Synonym | fatty-acid ester of hydroxy-fatty-acid hydrolase activity |
| Major function | Hydrolysis of the ester bond in FAHFAs to release a free fatty acid and a hydroxy fatty acid |
| Substrate | Fatty acid esters of hydroxy fatty acids (FAHFAs) |
| Products | Free fatty acid and hydroxy fatty acid |
| Representative enzymes | AIG1 and ADTRP (endogenous FAHFA hydrolases) |
| Opposing activity | ATGL (PNPLA2) catalyzes FAHFA biosynthesis |
| Biological context | FAHFA signaling in adipose tissue, inflammation, and metabolic regulation |
What Is GO:0120573?
GO:0120573 (FAHFA hydrolase activity) is defined as catalysis of the hydrolysis of the ester bond in a fatty acid ester of a hydroxy fatty acid (FAHFA), yielding a free fatty acid and a hydroxy fatty acid. In other words, it is the enzymatic function that breaks FAHFAs apart into their two fatty acid components. The synonym fatty-acid ester of hydroxy-fatty-acid hydrolase activity captures the same reaction. This term belongs to the molecular_function ontology aspect and describes the catalytic activity itself rather than the biological process or cellular location in which it occurs.
Why Is FAHFA hydrolase activity Important in Cell Biology?
GO:0120573 is important because it controls the abundance of FAHFAs, a family of endogenous bioactive lipids with signaling roles in insulin sensitivity, inflammation, and energy homeostasis. The identification of AIG1 and ADTRP as endogenous FAHFA hydrolases demonstrated that FAHFA turnover is enzymatically regulated and that loss of these hydrolases elevates FAHFA levels in mice. Because FAHFA levels are altered by fasting, acute inflammation, and diet-induced obesity, the enzymes that carry out GO:0120573 are directly relevant to metabolic disease research. Understanding this activity therefore provides a mechanistic handle on how cells tune lipid signaling.
• Controls steady-state levels of bioactive FAHFAs by hydrolyzing the ester bond that defines this lipid class.
• Provides the enzymatic counterbalance to ATGL-mediated FAHFA biosynthesis in adipose tissue.
• AIG1 and ADTRP knockout increases FAHFA abundance, showing that GO:0120573 is rate-contributing in vivo.
• Links FAHFA turnover to fasting responses in white adipose tissue.
• Connects FAHFA metabolism to acute inflammation in adipose tissue and differentiated adipocytes.
• Implicates FAHFA hydrolysis in diet-induced obesity and energy metabolism through caspase-6-related pathways.
• Enables activity-based profiling of serine hydrolases using fluorophosphonate-alkyne probes.
• Provides candidate targets for cardiometabolic disease research, including TFPI-related pathways.
• Supports development of CRISPR knockout and knock-in models to test causality of specific hydrolases.
• Offers a lipidomic readout for drug discovery aimed at modulating FAHFA signaling.
Molecular Mechanism of FAHFA hydrolase activity
Substrate recognition and binding
In simple terms: The enzyme first grabs the FAHFA molecule so it can cut the ester bond.
FAHFA hydrolases act on fatty acid esters of hydroxy fatty acids, a lipid class in which a fatty acid is esterified to a hydroxyl group on a second fatty acid backbone. The enzyme must recognize both the acyl chain and the hydroxy fatty acid portion to position the ester bond in the active site. AIG1 and ADTRP are the principal endogenous hydrolases that carry out this reaction in mice, and their substrate specificity defines which FAHFA regioisomers are hydrolyzed. Because FAHFAs are endogenous bioactive signaling lipids, substrate recognition is a key determinant of the signaling pool that remains intact.
Catalytic hydrolysis of the ester bond
In simple terms: The enzyme uses water to split the FAHFA into two fatty acid pieces.
The catalytic event of GO:0120573 is hydrolysis of the ester bond in a FAHFA, yielding a free fatty acid and a hydroxy fatty acid. AIG1 and ADTRP belong to the serine hydrolase superfamily, and their hydrolase activity is responsible for FAHFA turnover in vivo. This hydrolytic step is the direct molecular opposite of FAHFA biosynthesis, in which ATGL (PNPLA2) catalyzes ester bond formation. The balance between these two activities determines the steady-state concentration of FAHFAs in tissues such as white adipose tissue.
Enzyme families and activity-based profiling
In simple terms: Scientists use chemical probes to find which enzymes can cut FAHFAs.
AIG1 and ADTRP are the best-characterized endogenous FAHFA hydrolases, and their identification relied on biochemical and genetic approaches in mice. Activity-based probes such as fluorophosphonate-alkyne reagents covalently label serine hydrolases and enable profiling of candidate FAHFA hydrolases in complex proteomes. These probes are broadly reactive and cell permeable, making them useful for discovering additional enzymes that may execute GO:0120573. Such profiling complements genetic screens and lipidomic measurements of FAHFA species.
Regulation by metabolic state
In simple terms: How much FAHFA-cutting happens depends on whether the body is fasting, inflamed, or obese.
FAHFA levels and the enzymes that control them are regulated by metabolic state. ATGL-catalyzed biosynthesis mediates the upregulation of FAHFA levels in white adipose tissue with fasting, indicating that biosynthetic and hydrolytic arms are coordinately tuned. Acute inflammation upregulates FAHFAs in adipose tissue and in differentiated adipocytes, showing that inflammatory signals can shift the balance of FAHFA metabolism. Diet-induced obesity models further link FAHFA metabolism to caspase-6-dependent control of lipid and energy metabolism. Together, these findings indicate that GO:0120573 does not operate at a fixed rate but is modulated by physiological context.
Relationship to cardiometabolic pathways
In simple terms: FAHFA-cutting enzymes connect to broader heart and metabolic disease pathways.
FAHFA metabolism intersects with cardiometabolic disease biology. The androgen-dependent tissue factor pathway inhibitor regulating protein ADTRP, which is also a FAHFA hydrolase, has peripheral actions and associations with cardiometabolic diseases. This dual role highlights how a single serine hydrolase can participate in both lipid signaling and coagulation-related pathways. Understanding GO:0120573 therefore has implications beyond lipid biochemistry, extending into vascular and metabolic physiology.
Key Genes Involved in GO:0120573 FAHFA hydrolase activity
The following genes and proteins have been experimentally linked to FAHFA hydrolysis, FAHFA biosynthesis, or FAHFA-related metabolic regulation.
| Gene | Major Role | Research Relevance |
|---|---|---|
| AIG1 | Endogenous FAHFA hydrolase that catalyzes GO:0120573 | Knockout increases FAHFA levels; core enzyme for studying FAHFA turnover |
| ADTRP | Endogenous FAHFA hydrolase and TFPI-regulating protein | Links FAHFA hydrolysis to cardiometabolic disease and coagulation pathways |
| PNPLA2 (ATGL) | Biosynthetic enzyme for FAHFAs, opposing hydrolase activity | Key node for fasting-induced FAHFA upregulation in white adipose tissue |
| PRDX6 | Peroxiredoxin 6 implicated in FAHFA biosynthesis | Provides insight into biosynthetic routes that balance GO:0120573 |
| CASP6 | Caspase-6 controls lipid and energy metabolism in diet-induced obesity | Connects FAHFA metabolism to obesity-related signaling |
| TFPI | Tissue factor pathway inhibitor, regulated by ADTRP | Links FAHFA hydrolase biology to coagulation and cardiometabolic disease |
| ABHD family members | Serine hydrolases labeled by fluorophosphonate-alkyne probes | Candidate FAHFA hydrolases for profiling studies |
| Serine hydrolase superfamily | Enzymes with catalytic serine nucleophiles | Broad family containing AIG1, ADTRP, and related hydrolases |
| Lipid droplet proteins | Compartmentalize FAHFA biosynthesis and hydrolysis | Relevant to subcellular localization of FAHFA metabolism |
| Adipocyte signaling proteins | Mediate FAHFA responses in adipose tissue | Used to study inflammation-driven FAHFA changes |
| Insulin sensitivity pathways | FAHFAs are linked to glucose homeostasis | Provide functional readouts for hydrolase manipulation |
| Inflammatory signaling mediators | Upregulate FAHFAs in adipose tissue | Help define context-dependent regulation of GO:0120573 |
| Energy metabolism regulators | Control lipid and energy balance | Relevant to diet-induced obesity models |
| FAHFA biosynthetic enzymes | Generate FAHFAs that are substrates for GO:0120573 | Essential for interpreting hydrolase loss-of-function phenotypes |
| FAHFA receptor/signaling targets | Mediate downstream effects of FAHFAs | Help connect hydrolysis to physiological outcomes |
| Cardiometabolic risk genes | Associated with TFPI/ADTRP pathways | Candidate modifiers of FAHFA-related disease risk |
How Is FAHFA hydrolase activity Regulated?
FAHFA hydrolase activity is regulated at the level of substrate availability and metabolic state rather than by a single dedicated transcription factor. Fasting upregulates FAHFA levels in white adipose tissue through ATGL-catalyzed biosynthesis, which indirectly shifts the balance against hydrolysis. Acute inflammation also upregulates FAHFAs in adipose tissue and differentiated adipocytes, indicating that inflammatory cues can alter the flux through FAHFA metabolic pathways. In diet-induced obesity, caspase-6 controls lipid and energy metabolism, providing another layer of physiological regulation that may influence FAHFA turnover. The peroxiredoxin 6 pathway has been implicated in FAHFA biosynthesis, further shaping the substrate pool available to hydrolases. Together, these findings indicate that GO:0120573 is embedded in a dynamic metabolic network rather than being constitutively active.
FAHFA hydrolase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| AIG1 | FAHFA turnover and metabolic signaling | AIG1 knockout mouse or cell line with lipidomic readout |
| ADTRP | Cardiometabolic disease and TFPI regulation | ADTRP knockout with coagulation and lipid profiling |
| PNPLA2 (ATGL) | Fasting-induced FAHFA biosynthesis in adipose tissue | Adipose-specific knockout or overexpression |
| CASP6 | Diet-induced obesity and energy metabolism | Caspase-6 knockout in high-fat diet models |
| PRDX6 | FAHFA biosynthesis and redox biology | PRDX6 loss-of-function with FAHFA lipidomics |
Metabolic disease and insulin sensitivity
FAHFAs are endogenous bioactive lipids linked to insulin sensitivity and glucose homeostasis, and their levels are controlled by the balance between biosynthesis and hydrolysis. AIG1 and ADTRP knockout elevates FAHFA levels in mice, suggesting that reducing GO:0120573 activity could increase this beneficial lipid class. ATGL-mediated FAHFA biosynthesis is upregulated in white adipose tissue during fasting, further supporting a role for FAHFA metabolism in systemic energy balance. These observations make FAHFA hydrolases candidate targets for metabolic disease research.
Obesity and energy metabolism
Diet-induced obesity models have linked FAHFA metabolism to caspase-6-dependent control of lipid and energy metabolism. Because FAHFA levels are dynamically regulated in adipose tissue, enzymes executing GO:0120573 may influence obesity-related phenotypes. Acute inflammation upregulates FAHFAs in adipose tissue and differentiated adipocytes, connecting FAHFA turnover to inflammatory states that accompany obesity. These findings support further investigation of FAHFA hydrolases in obesity and its metabolic complications.
Cardiometabolic and vascular biology
ADTRP, one of the endogenous FAHFA hydrolases, is also known as the androgen-dependent tissue factor pathway inhibitor regulating protein, and its peripheral actions have been associated with cardiometabolic diseases. This dual function links GO:0120573 to coagulation-related and vascular pathways in addition to lipid signaling. Researchers studying cardiometabolic disease may therefore benefit from considering FAHFA hydrolysis as a contributing mechanism.
From FAHFA hydrolase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of a candidate gene increase FAHFA levels? | CRISPR knockout cell line or mouse with targeted lipidomics |
| Does a specific catalytic residue mediate FAHFA hydrolysis? | Point mutation of the predicted catalytic serine |
| Can a tagged hydrolase be tracked in cells? | Knock-in of an epitope or fluorescent tag |
| Does overexpression of a hydrolase reduce FAHFAs? | Stable overexpression in adipocyte or HEK293 cells |
| Which serine hydrolases are active in a tissue? | Activity-based protein profiling with fluorophosphonate-alkyne probes |
| How does fasting alter FAHFA metabolism? | In vivo fasting model with adipose lipidomics |
How to Study the FAHFA hydrolase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Targeted lipidomics | Abundance of FAHFA species | Quantifying products of GO:0120573 in cells or tissues |
| Activity-based protein profiling | Active serine hydrolases in a proteome | Discovering candidate FAHFA hydrolases |
| CRISPR knockout | Loss-of-function phenotype | Testing whether a gene controls FAHFA levels |
| Point mutation | Requirement for catalytic residues | Distinguishing hydrolase activity from scaffolding |
| Overexpression | Gain-of-function effect on FAHFAs | Testing sufficiency of a candidate hydrolase |
| Metabolic phenotyping | Insulin sensitivity and energy balance | Linking FAHFA hydrolysis to physiology |
| Fasting and feeding studies | Dynamic changes in FAHFA levels | Studying regulation of FAHFA metabolism |
| Inflammation models | FAHFA response to inflammatory stimuli | Connecting GO:0120573 to inflammation |
Lipidomics for FAHFA quantification
Targeted lipidomics is the primary method for measuring FAHFA species and determining whether a genetic perturbation changes the products of GO:0120573. By comparing FAHFA levels in wild-type and hydrolase-deficient samples, researchers can infer hydrolase activity in vivo. This approach has been used to show that AIG1 and ADTRP loss elevates FAHFAs in mice. Lipidomics is also essential for interpreting fasting and inflammation experiments in adipose tissue.
Activity-based protein profiling
Fluorophosphonate-alkyne probes covalently label serine hydrolases and enable activity-based protein profiling in complex proteomes. These probes are broadly reactive and cell permeable, making them suitable for identifying candidate FAHFA hydrolases. When combined with genetic perturbation, activity-based profiling can confirm that a specific enzyme contributes to GO:0120573. This method is particularly useful when the enzyme has no known substrate-specific antibody.
Genetic and CRISPR models
CRISPR knockout, point mutation, and knock-in models allow causal testing of candidate FAHFA hydrolases. Knockout of AIG1 or ADTRP increases FAHFA levels, providing direct evidence that these genes encode enzymes with GO:0120573 activity. Point mutations of catalytic residues can distinguish hydrolysis-dependent from scaffold functions. Overexpression models complement loss-of-function studies by testing whether increased hydrolase activity lowers FAHFA abundance.
Metabolic phenotyping
Because FAHFAs are linked to insulin sensitivity and energy metabolism, metabolic phenotyping is used alongside lipidomics to assess the physiological impact of altering GO:0120573. Fasting and diet-induced obesity models reveal dynamic regulation of FAHFA levels in white adipose tissue. Acute inflammation models further show that FAHFA metabolism responds to inflammatory cues. Together, these methods connect molecular hydrolase activity to organism-level metabolism.
How CRISPR Can Be Used to Study GO:0120573 FAHFA hydrolase activity
Knockout
CRISPR knockout of candidate FAHFA hydrolases such as AIG1 and ADTRP is used to test whether loss of the enzyme increases FAHFA levels, which would confirm its role in GO:0120573. Knockout models are also valuable for metabolic phenotyping, because FAHFAs are linked to insulin sensitivity and energy balance. In vivo knockout of AIG1 and ADTRP has provided direct evidence that these enzymes are endogenous FAHFA hydrolases. Knockout studies in adipose tissue can be combined with fasting or high-fat diet challenges to reveal context-dependent regulation.
Point Mutation
Point mutation of the predicted catalytic serine in a candidate serine hydrolase can determine whether enzymatic activity is required for FAHFA hydrolysis. By comparing wild-type and catalytically dead mutants, researchers can separate hydrolysis-dependent effects from protein-protein interaction effects. This approach is particularly useful for enzymes like AIG1 and ADTRP that belong to the serine hydrolase superfamily. Point mutants can also be used to validate activity-based probe labeling sites.
Knock-in
Knock-in of epitope or fluorescent tags allows tracking of FAHFA hydrolase localization and expression in cells and tissues. Tagged knock-in models can be used to immunoprecipitate the enzyme and measure its activity in vitro. They also enable imaging of subcellular localization relative to lipid droplets and other organelles involved in FAHFA metabolism. Knock-in of reporter alleles can provide readouts of hydrolase promoter activity under fasting or inflammatory conditions.
Overexpression
Overexpression of a candidate FAHFA hydrolase tests whether increased enzyme levels are sufficient to lower FAHFA abundance. This is a complementary approach to knockout, and together they establish causality in both directions. Overexpression in adipocyte cell lines or HEK293 cells can be combined with lipidomics to quantify changes in specific FAHFA species. Such models are also useful for testing whether a hydrolase can reverse FAHFA accumulation caused by biosynthetic enzyme overexpression.
How EDITGENE Supports FAHFA hydrolase activity Research
Researchers studying FAHFA hydrolase activity-related genes often need to determine whether a candidate gene is causally involved in FAHFA turnover or whether it merely correlates with changes in lipid abundance. Establishing causality requires precise genetic models in which the candidate gene is deleted, mutated, tagged, or overexpressed, followed by lipidomic and metabolic readouts. EDITGENE provides these models to accelerate FAHFA biology research.
Contact EDITGENE today to design your custom CRISPR model for FAHFA hydrolase activity research.
Frequently Asked Questions About FAHFA hydrolase activity
What is FAHFA hydrolase activity?
FAHFA hydrolase activity (GO:0120573) is the catalysis of the hydrolysis of the ester bond in a fatty acid ester of a hydroxy fatty acid (FAHFA), yielding a free fatty acid and a hydroxy fatty acid.
What genes are involved in FAHFA hydrolase activity?
AIG1 and ADTRP are the principal endogenous FAHFA hydrolases identified in mice, while ATGL (PNPLA2) catalyzes the opposing biosynthetic reaction.
What is the GO ID for FAHFA hydrolase activity?
The GO ID for FAHFA hydrolase activity is GO:0120573, and it belongs to the molecular_function ontology aspect.
How are FAHFAs regulated by fasting?
ATGL-catalyzed biosynthesis mediates the upregulation of FAHFA levels in white adipose tissue with fasting.
Do FAHFAs change during inflammation?
Acute inflammation upregulates FAHFAs in adipose tissue and in differentiated adipocytes.
What diseases are linked to FAHFA metabolism?
FAHFA metabolism has been linked to metabolic disease, obesity, and cardiometabolic conditions through pathways involving AIG1, ADTRP, ATGL, and caspase-6.
How can I study FAHFA hydrolase activity in the lab?
Targeted lipidomics, activity-based protein profiling with fluorophosphonate-alkyne probes, and CRISPR knockout or overexpression models are commonly used.
What is the role of ADTRP in FAHFA metabolism?
ADTRP is an endogenous FAHFA hydrolase and also functions as the androgen-dependent tissue factor pathway inhibitor regulating protein associated with cardiometabolic diseases.
Is ATGL a FAHFA hydrolase or a biosynthetic enzyme?
ATGL (PNPLA2) acts as a biosynthetic enzyme for FAHFAs, opposing the hydrolytic activity of AIG1 and ADTRP.
Can CRISPR be used to study FAHFA hydrolases?
Yes, CRISPR knockout, point mutation, knock-in, and overexpression models are used to test whether candidate genes causally regulate FAHFA levels.
Conclusion
GO:0120573 (FAHFA hydrolase activity) defines the enzymatic reaction that breaks down FAHFAs into free fatty acids and hydroxy fatty acids, and it is executed by endogenous hydrolases such as AIG1 and ADTRP. This activity opposes ATGL-mediated FAHFA biosynthesis and is dynamically regulated by fasting, inflammation, and diet-induced obesity. Because FAHFAs are bioactive signaling lipids linked to insulin sensitivity and cardiometabolic disease, the enzymes of GO:0120573 are promising targets for metabolic research. Studying GO:0120573 requires a combination of lipidomics, activity-based protein profiling, and precise CRISPR models. EDITGENE supports this workflow with knockout, point mutation, knock-in, overexpression, and screening services tailored to FAHFA biology.
References
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- 3. Erikci Ertunc M et al.. 2020. AIG1 and ADTRP are endogenous hydrolases of fatty acid esters of hydroxy fatty acids (FAHFAs) in mice.. J Biol Chem 295(18):5891-5905 PMID: 32152231
- 4. Santoro A et al.. 2026. ATGL-catalyzed biosynthesis mediates the upregulation of fatty acid hydroxy fatty acids (FAHFA) levels in white adipose tissue with fasting.. J Biol Chem 302(3):111169 PMID: 41570983
- 5. Gupta A et al.. 2026. Caspase-6 Controls Lipid and Energy Metabolism in Diet-Induced Obesity.. Adv Sci (Weinh) 13(21):e14784 PMID: 41969066
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