GO:0120503 medium-chain fatty acid omega-1 hydroxylase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0120503 describes the catalytic conversion of an (omega-1)-ethyl medium-chain fatty acid (6-12 carbons) to its (omega-1)-hydroxy form using O2 and reduced NADPH-hemoprotein reductase [1, 2].
• This activity is a sub-terminal oxidation reaction, distinct from terminal omega-hydroxylation, and is carried out by cytochrome P450 enzymes such as CYP2S1 and CYP4B1 [2, 5].
• Medium-chain fatty acid omega-1 hydroxylation generates bioactive lipids that can influence inflammation, membrane remodeling, and metabolic signaling [2, 8].
• The reaction requires a redox partner (NADPH-hemoprotein reductase) to shuttle electrons from NADPH to the P450 heme iron [1, 3].
• Dysregulation of omega-1 hydroxylation has been linked to alcoholic liver disease, nephrotic syndrome, and altered fatty acid metabolism in kidney tissue [1, 4].
• CRISPR-based knockout, knock-in, and overexpression models are essential to dissect the physiological roles of enzymes exhibiting this activity [5, 6].
Description
Medium-chain fatty acid omega-1 hydroxylase activity (GO:0120503) is a molecular function that catalyzes the hydroxylation of medium-chain fatty acids at the carbon adjacent to the terminal methyl group (the omega-1 position). This reaction converts an (omega-1)-ethyl medium-chain fatty acid into an (omega-1)-hydroxy-medium-chain fatty acid, consuming molecular oxygen and reducing equivalents from NADPH via a hemoprotein reductase [1, 2]. The term is classified under molecular_function in the Gene Ontology and is defined by the chemical transformation rather than by any single gene product. Researchers study this activity because it represents a critical branch point in fatty acid metabolism, generating hydroxylated lipid mediators that participate in cellular signaling, detoxification, and membrane homeostasis [2, 8]. The enzymes responsible for this activity belong primarily to the cytochrome P450 superfamily, which are heme-thiolate proteins capable of oxidizing a vast array of endogenous and exogenous substrates [3, 5]. In humans, CYP2S1 has been shown to perform omega-1 hydroxylation of polyunsaturated fatty acids, while CYP4B1 exhibits omega-1 hydroxylation toward various fatty acids and xenobiotics [2, 5]. The reaction is also observed in experimental models of alcoholic liver disease, where dietary fatty acids modulate omega- and (omega-1)-hydroxylation activities. In the kidney, disorders of fatty acid metabolism in nephrotic rats involve altered hydroxylation pathways, suggesting a role for these enzymes in renal pathophysiology. Understanding GO:0120503 is therefore relevant for researchers in lipid biochemistry, pharmacology, and metabolic disease. The activity influences the balance between terminal and sub-terminal oxidation, which can determine whether fatty acids are directed toward energy production, storage, or the synthesis of signaling molecules [2, 8]. Because medium-chain fatty acids are increasingly used in clinical nutrition and as precursors for industrial chemicals, characterizing the enzymes and regulatory mechanisms behind omega-1 hydroxylation has both biomedical and biotechnological importance [6, 7].
medium-chain fatty acid omega-1 hydroxylase activity At A Glance
| GO ID | GO:0120503 |
|---|---|
| GO term | medium-chain fatty acid omega-1 hydroxylase activity |
| Ontology | molecular_function |
| Synonym | none |
| Major function | Catalyzes the omega-1 hydroxylation of medium-chain fatty acids (6-12 carbons) using O2 and reduced NADPH-hemoprotein reductase [1, 2]. |
| Reaction | an (omega-1)-ethyl medium-chain fatty acid + O2 + reduced [NADPH-hemoprotein reductase] = an (omega-1)-hydroxy-medium-chain fatty acid + H+ + H2O + oxidized [NADPH-hemoprotein reductase]. |
| Cofactors | Heme iron (in cytochrome P450 enzymes) and NADPH-hemoprotein reductase as electron donor [3, 5]. |
| Representative enzymes | CYP2S1, CYP4B1, and other cytochrome P450 family members [2, 5]. |
| Associated diseases | Alcoholic liver disease, nephrotic syndrome, and disorders of fatty acid metabolism [1, 4]. |
What Is GO:0120503?
GO:0120503, medium-chain fatty acid omega-1 hydroxylase activity, is defined as the catalysis of the reaction: an (omega-1)-ethyl medium-chain fatty acid + O2 + reduced [NADPH-hemoprotein reductase] = an (omega-1)-hydroxy-medium-chain fatty acid + H+ + H2O + oxidized [NADPH-hemoprotein reductase]. A medium-chain fatty acid has an aliphatic tail containing 6 to 12 carbons. In simpler terms, this activity adds a hydroxyl group to the second-to-last carbon of a medium-chain fatty acid, using oxygen and NADPH as co-substrates [1, 2].
Why Is medium-chain fatty acid omega-1 hydroxylase activity Important in Cell Biology?
Medium-chain fatty acid omega-1 hydroxylase activity is important because it generates hydroxylated fatty acids that serve as signaling molecules and metabolic intermediates, influencing pathways related to inflammation, membrane fluidity, and energy homeostasis [2, 8]. The reaction also represents a route for the detoxification and biotransformation of medium-chain fatty acids and related xenobiotics, with implications for drug metabolism and toxicology. In disease contexts, altered omega-1 hydroxylation has been observed in experimental alcoholic liver disease and in kidney disorders, suggesting that this activity contributes to the pathogenesis of metabolic and renal conditions [1, 4]. Furthermore, the enzymes catalyzing this reaction are potential targets for engineering biocatalysts for the production of fine chemicals and pharmaceuticals [6, 7].
• Generates (omega-1)-hydroxy medium-chain fatty acids that can act as lipid mediators in inflammation and cell signaling [2, 8].
• Provides a metabolic route for the oxidation of medium-chain fatty acids, affecting energy balance and membrane lipid composition [1, 4].
• Involved in the biotransformation of xenobiotics and drugs, particularly through cytochrome P450 enzymes like CYP4B1.
• Dysregulated in alcoholic liver disease, where dietary fatty acids modulate omega- and (omega-1)-hydroxylation activities.
• Altered in kidney disorders such as puromycin aminonucleoside-induced nephrotic syndrome in rats.
• Enzymes with this activity, such as CYP2S1, are implicated in polyunsaturated fatty acid metabolism and may influence cancer and inflammation.
• The reaction requires NADPH-hemoprotein reductase, linking it to cellular redox status and NADPH availability.
• Biotechnological potential for selective oxyfunctionalization of alkyl esters and alkanes using engineered enzymes [6, 7].
• Provides a target for CRISPR-based knockout and knock-in studies to elucidate gene function in lipid metabolism [5, 6].
• Relevant to nutritional studies on medium-chain triglycerides and their metabolic fate [1, 4].
What Happens During medium-chain fatty acid omega-1 hydroxylase activity?
Substrate binding and orientation
In simple terms: The enzyme grabs a medium-chain fatty acid and positions it so that the second-to-last carbon is close to the reactive heme iron.
The catalytic cycle begins when a medium-chain fatty acid (6-12 carbons) binds within the active site of a cytochrome P450 enzyme. The substrate is oriented such that the omega-1 carbon, which is the carbon adjacent to the terminal methyl group, is positioned near the heme iron. This orientation is critical for determining whether hydroxylation occurs at the omega-1 position rather than at the terminal omega position [2, 5]. For example, CYP2S1 preferentially hydroxylates polyunsaturated fatty acids at the omega-1 position, as demonstrated by untargeted metabolomic approaches. Similarly, CYP4B1 can perform omega-1 hydroxylation on various substrates, although its regioselectivity can vary depending on the substrate structure.
Electron transfer from NADPH
In simple terms: A partner protein delivers electrons from NADPH to the heme iron, activating oxygen for the reaction.
The hydroxylation reaction requires two electrons, which are supplied by NADPH via the redox partner NADPH-hemoprotein reductase (also known as cytochrome P450 reductase). The reductase binds to the P450 enzyme and transfers electrons from NADPH to the heme iron, reducing it from the ferric (Fe3+) to the ferrous (Fe2+) state. This reduction enables the binding and activation of molecular oxygen [1, 3]. The stoichiometry of the reaction includes the consumption of one molecule of O2 and one molecule of reduced NADPH-hemoprotein reductase per hydroxylated product, with the concomitant release of water and oxidized reductase.
Oxygen activation and hydroxylation
In simple terms: Oxygen is split, and one oxygen atom is inserted into the fatty acid at the omega-1 carbon, while the other becomes water.
Once the heme iron is reduced and oxygen is bound, the reaction proceeds through a series of steps that generate a highly reactive iron-oxo species (Compound I). This species abstracts a hydrogen atom from the omega-1 carbon of the fatty acid, forming a substrate radical. The radical then recombines with the iron-bound hydroxyl group, resulting in the insertion of a hydroxyl group at the omega-1 position. The other oxygen atom is reduced to water. The product, an (omega-1)-hydroxy-medium-chain fatty acid, is released from the active site [1, 2]. This mechanism is characteristic of cytochrome P450 monooxygenases and is supported by studies on CYP2S1 and CYP4B1 [2, 5].
Product release and regeneration
In simple terms: The hydroxylated fatty acid leaves the enzyme, and the enzyme is ready to start another cycle.
After the hydroxylated product is released, the enzyme returns to its resting state, ready to bind another substrate molecule. The oxidized NADPH-hemoprotein reductase is recycled by cellular reductases to its reduced form, maintaining the supply of electrons for subsequent cycles [1, 3]. The overall reaction is: an (omega-1)-ethyl medium-chain fatty acid + O2 + reduced [NADPH-hemoprotein reductase] = an (omega-1)-hydroxy-medium-chain fatty acid + H+ + H2O + oxidized [NADPH-hemoprotein reductase]. The efficiency of this cycle can be influenced by the availability of NADPH, the expression levels of the P450 enzyme and its reductase partner, and the presence of inhibitors or alternative substrates [3, 5].
Key Genes Involved in GO:0120503 medium-chain fatty acid omega-1 hydroxylase activity
The following genes encode enzymes or associated proteins that exhibit or support medium-chain fatty acid omega-1 hydroxylase activity, based on published biochemical and genetic studies.
| Gene | Major Role | Research Relevance |
|---|---|---|
| CYP2S1 | Cytochrome P450 enzyme that catalyzes omega-1 hydroxylation of polyunsaturated fatty acids. | Studied for its role in fatty acid metabolism and potential implications in inflammation and cancer. |
| CYP4B1 | Cytochrome P450 enzyme with omega-1 hydroxylase activity toward fatty acids and xenobiotics. | Model for understanding substrate specificity and regioselectivity in P450 enzymes. |
| CYP4A11 | Major lauric acid omega-hydroxylase in human liver; may also contribute to omega-1 hydroxylation. | Used as a reference for comparing omega versus omega-1 regioselectivity. |
| POR | NADPH-hemoprotein reductase; transfers electrons from NADPH to cytochrome P450 enzymes [1, 3]. | Essential for reconstituting hydroxylase activity in vitro and in cell models. |
| ALKBGT | Alkane hydroxylase from Pseudomonas putida GPo1; can perform omega-oxyfunctionalization of alkyl esters. | Biotechnological model for selective oxyfunctionalization. |
| AlkL | Outer membrane protein from P. putida GPo1 that facilitates substrate access for AlkBGT. | Used in engineered E. coli for whole-cell biocatalysis. |
| CYP4A | Subfamily of cytochrome P450 enzymes involved in fatty acid omega-hydroxylation. | Target for studying fatty acid metabolism in liver and kidney [3, 4]. |
| CYP2E1 | Ethanol-inducible P450 that can contribute to fatty acid hydroxylation. | Linked to alcoholic liver disease and oxidative stress. |
| CYP4F | Subfamily involved in leukotriene B4 omega-hydroxylation, related to omega-1 activity. | Model for understanding substrate recognition in eicosanoid metabolism. |
| LTB4 | Leukotriene B4; substrate for omega- and omega-1 hydroxylases. | Used to assay hydroxylase activity in hepatic microsomes. |
| PPAR-alpha | Nuclear receptor that regulates fatty acid oxidation genes. | Potential upstream regulator of hydroxylase expression in kidney and liver. |
| HNF4-alpha | Transcription factor controlling liver-specific gene expression, including P450 genes. | May regulate CYP4A11 and other hydroxylases. |
| Nrf2 | Transcription factor involved in antioxidant response; may influence P450 expression. | Studied in context of xenobiotic metabolism. |
| AHR | Aryl hydrocarbon receptor; regulates CYP1 family but may crosstalk with fatty acid metabolism. | Relevant for understanding xenobiotic-endobiotic interactions. |
| CAR | Constitutive androstane receptor; regulates drug-metabolizing enzymes. | Potential regulator of hydroxylase genes. |
| PXR | Pregnane X receptor; regulates xenobiotic metabolism. | May affect expression of P450 enzymes with omega-1 activity. |
How Is medium-chain fatty acid omega-1 hydroxylase activity Regulated?
The expression and activity of enzymes exhibiting medium-chain fatty acid omega-1 hydroxylase activity are regulated at multiple levels. Transcriptional regulation involves nuclear receptors such as PPAR-alpha, HNF4-alpha, CAR, and PXR, which respond to fatty acids, xenobiotics, and metabolic signals [3, 5]. For example, in experimental alcoholic liver disease, dietary fatty acids modulate omega- and (omega-1)-hydroxylation activities, suggesting that lipid composition influences enzyme expression or activity. In the kidney of nephrotic rats, disorders of fatty acid metabolism are associated with altered hydroxylation, potentially through PPAR-alpha signaling. Post-translational regulation includes competition for NADPH-hemoprotein reductase, which is shared among many P450 enzymes, and feedback inhibition by products. Additionally, the redox state of the cell, particularly the NADPH/NADP+ ratio, can affect the reaction rate.
medium-chain fatty acid omega-1 hydroxylase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| CYP2E1 | Alcoholic liver disease; oxidative stress | Cyp2e1 knockout mice fed ethanol-containing diets |
| CYP4A11 | Fatty acid metabolism; hypertension | CYP4A11 overexpression in HepG2 cells |
| CYP2S1 | Inflammation; cancer | CYP2S1 knockout cell lines and xenograft models |
| CYP4B1 | Xenobiotic metabolism; lung toxicity | CYP4B1 transgenic mice |
| LTB4 hydroxylase | Inflammatory diseases | Microsomal assays from liver tissue |
Alcoholic liver disease
Experimental alcoholic liver disease is associated with changes in fatty acid omega- and (omega-1)-hydroxylation activities, which vary depending on the dietary fatty acid composition. Chronic ethanol consumption can induce CYP2E1 and other P450 enzymes, potentially altering the balance of hydroxylated metabolites and contributing to oxidative stress and liver injury. The omega-1 hydroxylation pathway may influence the generation of bioactive lipids that modulate inflammation and fibrosis in the liver.
Kidney disorders and nephrotic syndrome
In puromycin aminonucleoside-induced nephrotic rats, disorders of fatty acid metabolism in the kidney include altered hydroxylation pathways. The kidney relies on fatty acid oxidation for energy, and perturbations in omega-1 hydroxylation may affect lipid homeostasis and contribute to renal dysfunction. These findings suggest that enzymes with this activity could be potential targets for therapeutic intervention in kidney diseases associated with lipid metabolic disorders.
Inflammation and eicosanoid metabolism
Medium-chain fatty acid omega-1 hydroxylase activity is related to the broader family of fatty acid hydroxylases that metabolize eicosanoids such as leukotriene B4. Hepatic microsomal leukotriene B4 hydroxylases catalyze omega- and omega-1 hydroxylation, which inactivates pro-inflammatory leukotrienes. Therefore, alterations in omega-1 hydroxylation could impact inflammatory responses and resolution. CYP2S1, which exhibits omega-1 hydroxylase activity toward polyunsaturated fatty acids, may also play a role in modulating inflammation through lipid mediator production.
From medium-chain fatty acid omega-1 hydroxylase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of CYP2S1 alter omega-1 hydroxylation of polyunsaturated fatty acids? | CYP2S1 knockout cell line (e.g., HepG2) generated by CRISPR |
| What is the effect of a specific point mutation in the CYP4B1 active site on regioselectivity? | Point-mutation knock-in in HEK293 cells |
| Can we tag endogenous CYP4A11 to study its localization and interaction with POR? | Knock-in of FLAG or GFP tag at the CYP4A11 locus |
| Does overexpression of CYP2S1 protect against inflammation in vitro? | CYP2S1 overexpression in macrophages or epithelial cells |
| What is the impact of CYP4B1 knockout on xenobiotic-induced toxicity? | CYP4B1 knockout mouse model |
| Can engineered AlkBGT/AlkL improve omega-1 oxyfunctionalization of alkyl esters? | E. coli expressing AlkBGT and AlkL variants |
How to Study the medium-chain fatty acid omega-1 hydroxylase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| LC-MS/MS-based enzyme assay | Hydroxylated fatty acid products | Quantifying omega-1 hydroxylase activity in microsomes [1, 2] |
| Untargeted metabolomics | Global changes in lipid metabolites | Identifying novel substrates and pathways |
| qRT-PCR | mRNA expression of P450 genes | Assessing transcriptional regulation [1, 4] |
| Western blot | Protein levels of hydroxylases | Validating expression changes [3, 5] |
| CRISPR knockout | Loss-of-function phenotype | Determining gene necessity for activity [2, 5] |
| CRISPR knock-in | Tagged or mutant protein expression | Studying localization and function [3, 5] |
| Heterologous expression | Recombinant enzyme activity | Biocatalyst development [6, 7] |
| Microsomal incubation | Intrinsic clearance and metabolite profiling | Drug metabolism studies [3, 8] |
Enzyme activity assays
Direct measurement of medium-chain fatty acid omega-1 hydroxylase activity typically uses microsomal fractions or recombinant enzymes incubated with a radiolabeled or fluorescently labeled medium-chain fatty acid substrate, NADPH, and NADPH-hemoprotein reductase. Products are separated by HPLC or LC-MS and quantified [1, 3]. For example, lauric acid omega-hydroxylation is assayed in human liver microsomes to determine CYP4A11 activity. Similar assays can be adapted to measure omega-1 hydroxylation by using substrates that favor this regiochemistry or by detecting the specific (omega-1)-hydroxy product.
Metabolomic profiling
Untargeted metabolomics using LC-MS/MS can identify and quantify hydroxylated fatty acid metabolites in biological samples, revealing the contribution of omega-1 hydroxylation to the lipidome. This approach was used to demonstrate the role of CYP2S1 in polyunsaturated fatty acid omega-1 hydroxylation. By comparing wild-type and knockout cells or tissues, researchers can map the metabolic pathways affected by the enzyme.
Gene expression analysis
Quantitative RT-PCR, RNA-seq, and Western blotting are used to measure the expression levels of genes encoding enzymes with this activity, such as CYP2S1, CYP4B1, and CYP4A11, under different physiological or pathological conditions [1, 4]. For instance, in alcoholic liver disease models, changes in CYP2E1 and CYP4A expression are correlated with hydroxylase activity. In nephrotic rats, kidney fatty acid metabolism genes are dysregulated, which can be assessed by transcriptomics.
CRISPR-based genetic models
CRISPR/Cas9 knockout, point mutation, and knock-in strategies enable precise manipulation of genes encoding omega-1 hydroxylases to study their function in cell lines and animal models [5, 6]. For example, knockout of CYP2S1 in human cells can confirm its role in omega-1 hydroxylation and downstream biological effects. Overexpression of CYP4B1 or AlkBGT in E. coli can be used for biotransformation studies [5, 6].
How CRISPR Can Be Used to Study GO:0120503 medium-chain fatty acid omega-1 hydroxylase activity
Knockout
CRISPR/Cas9-mediated knockout of genes encoding medium-chain fatty acid omega-1 hydroxylases, such as CYP2S1 or CYP4B1, allows researchers to abolish enzyme activity and assess its contribution to lipid metabolism, inflammation, and disease phenotypes [2, 5]. Knockout cell lines can be used in metabolomic and lipidomic studies to identify endogenous substrates and products. In vivo knockout models, such as Cyp4b1-/- mice, can reveal systemic effects on fatty acid homeostasis and xenobiotic toxicity.
Point Mutation
Point mutations introduced by CRISPR base editing or homology-directed repair can alter specific amino acid residues in the active site of omega-1 hydroxylases to probe substrate specificity and catalytic mechanism. For example, mutating residues in CYP4B1 that determine regioselectivity can shift the reaction from omega-1 to omega hydroxylation. Such models are valuable for understanding structure-function relationships and for engineering enzymes with desired properties [5, 7].
Knock-in
Knock-in of epitope tags (e.g., FLAG, HA) or fluorescent proteins (e.g., GFP) at the endogenous locus of a hydroxylase gene enables real-time tracking of protein expression, localization, and interaction with redox partners like NADPH-hemoprotein reductase. Knock-in of disease-associated mutations can model human genetic variants affecting enzyme activity. These models are essential for studying the spatiotemporal regulation of omega-1 hydroxylation in living cells.
Overexpression
CRISPR activation (CRISPRa) or traditional cDNA overexpression can drive high-level expression of omega-1 hydroxylases to enhance reaction rates for biochemical characterization or biotechnological production [6, 7]. Overexpression in E. coli of AlkBGT and AlkL, for instance, enables selective omega-oxyfunctionalization of alkyl esters. In mammalian cells, overexpression of CYP2S1 can amplify omega-1 hydroxylation of polyunsaturated fatty acids, facilitating downstream signaling studies.
How EDITGENE Supports medium-chain fatty acid omega-1 hydroxylase activity Research
Researchers studying medium-chain fatty acid omega-1 hydroxylase activity-related genes often need to determine whether a candidate gene is causally involved in lipid metabolism, inflammation, or disease. EDITGENE provides a comprehensive suite of CRISPR-based services to generate precisely engineered cell models, enabling functional validation of genes encoding omega-1 hydroxylases and their regulators.
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Frequently Asked Questions About medium-chain fatty acid omega-1 hydroxylase activity
What is medium-chain fatty acid omega-1 hydroxylase activity?
It is a molecular function (GO:0120503) that catalyzes the addition of a hydroxyl group to the omega-1 carbon of a medium-chain fatty acid (6-12 carbons), using O2 and NADPH-hemoprotein reductase [1, 2].
What genes are involved in medium-chain fatty acid omega-1 hydroxylase activity?
Genes encoding cytochrome P450 enzymes such as CYP2S1, CYP4B1, and CYP4A11, as well as the redox partner POR (NADPH-hemoprotein reductase), are involved [2, 3, 5].
Which enzymes catalyze omega-1 hydroxylation of fatty acids?
Cytochrome P450 enzymes, including CYP2S1 and CYP4B1, are known to catalyze omega-1 hydroxylation of various fatty acids [2, 5].
What is the difference between omega and omega-1 hydroxylation?
Omega hydroxylation adds a hydroxyl group to the terminal methyl carbon, while omega-1 hydroxylation adds it to the adjacent carbon. The two reactions are catalyzed by different P450 enzymes or by the same enzyme with different regioselectivity [2, 3].
How is medium-chain fatty acid omega-1 hydroxylase activity measured?
It is typically measured using LC-MS/MS or HPLC-based assays with microsomes or recombinant enzymes, detecting the (omega-1)-hydroxy product [1, 2].
What diseases are associated with defects in omega-1 hydroxylation?
Altered omega-1 hydroxylation has been observed in alcoholic liver disease, nephrotic syndrome, and inflammatory conditions [1, 4, 8].
Can CRISPR be used to study medium-chain fatty acid omega-1 hydroxylase activity?
Yes, CRISPR knockout, knock-in, and overexpression models enable precise manipulation of genes encoding these enzymes to study their function and regulation [2, 5, 6].
What is the role of NADPH-hemoprotein reductase in this activity?
NADPH-hemoprotein reductase transfers electrons from NADPH to the cytochrome P450 heme iron, which is essential for oxygen activation and substrate hydroxylation [1, 3].
Are there biotechnological applications of omega-1 hydroxylases?
Yes, engineered enzymes like AlkBGT from Pseudomonas putida are used for selective oxyfunctionalization of alkyl esters and alkanes in industrial biocatalysis [6, 7].
How does diet influence medium-chain fatty acid omega-1 hydroxylase activity?
Dietary fatty acid composition can modulate omega- and (omega-1)-hydroxylation activities, as shown in experimental alcoholic liver disease models.
Conclusion
Medium-chain fatty acid omega-1 hydroxylase activity (GO:0120503) is a specialized lipid-modifying function carried out by cytochrome P450 enzymes such as CYP2S1 and CYP4B1. It generates hydroxylated fatty acids that participate in cellular signaling, detoxification, and metabolic regulation, with implications for liver disease, kidney disorders, and inflammation [1, 2, 4, 5, 8]. Understanding the enzymes, cofactors, and regulatory mechanisms behind this activity requires integrated approaches including biochemical assays, metabolomics, and CRISPR-based genetic models. EDITGENE's services empower researchers to dissect this pathway with precision, from knockout and knock-in cell lines to library screening and bioinformatics support.
References
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- 3. Powell PK et al.. 1996. Identification of CYP4A11 as the major lauric acid omega-hydroxylase in human liver microsomes.. Arch Biochem Biophys 335(1):219-26 PMID: 8914854
- 4. Muroya Y et al.. 2012. Disorder of fatty acid metabolism in the kidney of PAN-induced nephrotic rats.. Am J Physiol Renal Physiol 303(7):F1070-9 PMID: 22874759
- 5. Baer BR et al.. 2006. CYP4B1: an enigmatic P450 at the interface between xenobiotic and endobiotic metabolism.. Drug Metab Rev 38(3):451-76 PMID: 16877261
- 6. van Nuland YM et al.. 2016. Application of AlkBGT and AlkL from Pseudomonas putida GPo1 for Selective Alkyl Ester ω-Oxyfunctionalization in Escherichia coli.. Appl Environ Microbiol 82(13):3801-3807 PMID: 27084021
- 7. Glieder A et al.. 2002. Laboratory evolution of a soluble, self-sufficient, highly active alkane hydroxylase.. Nat Biotechnol 20(11):1135-9 PMID: 12368811
- 8. Romano MC et al.. 1987. Biochemical characterization of hepatic microsomal leukotriene B4 hydroxylases.. J Biol Chem 262(4):1590-5 PMID: 3027095
