# Peroxisomes: Definition, Structure, Functions and Biogenesis > Learn what peroxisomes are, their structure and major functions in lipid metabolism and redox control, how they form, their roles in plants, and related... Canonical URL: https://biologynotesonline.com/peroxisomes-structure-enzymes-and-functions/ Author: Sourav Pan Last updated: September 12, 2026 ![Peroxisomes: Definition, Structure, Functions and Biogenesis](https://biologynotesonline.com/wp-content/uploads/2024/04/Structure-of-a-Peroxisome.webp) Peroxisomes are small cytoplasmic organelles belonging to the [microbody family](https://biologynotesonline.com/microbodies/). They are present in most eukaryotic cells and are found in the cytoplasm. Each peroxisome is enclosed by a single membrane (one surrounding lipid bilayer). They do not possess their own DNA and ribosomes. The name “peroxisome” is based on hydrogen peroxide (H₂O₂) metabolism. Oxidase enzymes inside these organelles can produce H₂O₂, while catalase present in the same organelle breaks it down. J. Rhodin first described such structures as “microbodies” in mouse kidney cells in 1954, while Christian de Duve later proposed the term peroxisome in 1965 after their H₂O₂-related activity was recognized. Peroxisomes are not exactly same in all cells. In plants, glyoxysomes are specialized forms of peroxisomes (particularly in germinating oil-rich seeds), and not a separate basic organelle type. ## Where are peroxisomes found? - Peroxisomes are found in almost all eukaryotic cells. These are present in animals, plants, fungi and also in many protists. - In animal cells, they are present in different tissues. However, the number of peroxisomes is not same in all cells and they are particularly abundant in liver and kidney cells. - Peroxisomes are also widely distributed in plant tissues, and their forms may change with tissue and developmental stage. In leaves, leaf peroxisomes are present. Germinating oil-rich seeds contain specialized peroxisomes known as glyoxysomes, while other specialized forms are found in roots and senescing tissues. - Yeasts and other fungi also contain peroxisomes. They are found in many unicellular eukaryotes as well, but their enzyme contents and metabolic activities can vary from one organism to another. - Peroxisomes are absent in prokaryotic cells (bacteria and archaea). It is a membrane-bound organelle found in eukaryotic cells. ## Characteristics of Peroxisomes - Peroxisomes are small organelles, generally spherical or oval with a diameter ranging from 0.1–1 µm. - They are found in the cytoplasm of nearly all eukaryotic cells. - They also have a single membrane layer (one phospholipid bilayer). Inside the membrane, a protein-rich granulated matrix is present. - Peroxisomes do not have their own DNA and ribosomes. Most of its proteins are synthesized in the cytosol and then brought into the organelle. - Most matrix proteins enter after their synthesis. Peroxisomal targeting signals (PTS) and peroxins (PEX proteins) are involved in bringing these proteins into peroxisomes. - Different oxidative enzymes are present within them. Hydrogen peroxide (H₂O₂) is formed during many of these reactions, which is broken down mainly by catalase. - Fatty acid oxidation is one of the major metabolic activities of peroxisomes. Other lipid and oxidative reactions also take place. - The enzyme composition is not same in every cell. It varies with the organism, tissue and metabolic condition. - Peroxisomes are highly dynamic structures. Their size, shape and number can change, and new peroxisomes may also form from already existing ones with contribution from the endoplasmic reticulum (ER). - Glyoxysomes are specialized peroxisomes found in plants, especially in germinating oil-storing seeds. They contain enzymes for fatty acid oxidation and the glyoxylate cycle. ## Structure of peroxisomes ![Cutaway diagram of a peroxisome showing its single membrane, enzyme-rich matrix, membrane proteins, and optional crystalloid structure.](https://biologynotesonline.com/wp-content/uploads/2024/04/Structure-of-a-Peroxisome-1024x768.webp)Cutaway diagram of a peroxisome showing its single membrane, enzyme-rich matrix, membrane proteins, and optional crystalloid structure. - Peroxisomes are small, usually spherical or oval shaped organelles having a diameter of about 0.1-1 µm. Their size and shape are not always fixed and some peroxisomes can become elongated or tubular depending on the cell. - They are surrounded by a single phospholipid membrane. A second membrane is absent, unlike mitochondria and chloroplasts. - Inside this membrane, a dense and finely granular matrix is present which contains the peroxisomal proteins and different metabolic enzymes. The matrix can be tightly packed. - In some peroxisomes, the proteins present in the matrix form a dense crystalline core (crystalloid). This internal structure is not found in all peroxisomes and differs according to organism and cell type. - The surrounding membrane also contains different peroxisomal membrane proteins (PMPs). These proteins are placed within the membrane and are involved in maintaining the peroxisomal membrane and movement of molecules across it. - Peroxisomes contain no DNA and ribosomes of their own. Hence, proteins required for its matrix and membrane are produced outside the peroxisome and then imported into the organelle. ## Peroxisomal Enzymes Peroxisomes contain different oxidative and metabolic enzymes in the matrix and membrane. The following are some of the important peroxisomal enzymes- - Catalase- It is a heme-containing enzyme which breaks down hydrogen peroxide (H₂O₂). The H₂O₂ produced during different oxidation reactions is converted into water and oxygen. - Acyl-CoA oxidase (ACOX)- The first reaction of peroxisomal β-oxidation is carried out by this enzyme. ACOX1 mainly acts on very-long-chain fatty acids (VLCFAs) and dicarboxylic fatty acids. ACOX2 acts on some branched-chain fatty acids and bile acid intermediates, and H₂O₂ is produced during oxidation. - D-bifunctional protein (DBP)- It is encoded by the HSD17B4 gene. Two reactions of β-oxidation are carried out by this enzyme, first hydration of enoyl-CoA and then its dehydrogenation. - Peroxisomal thiolase- ACAA1 and sterol carrier protein X (SCPx) are involved in the final step of peroxisomal β-oxidation. In this step, 3-ketoacyl-CoA is cleaved to form acetyl-CoA and a shortened acyl-CoA molecule. - Phytanoyl-CoA 2-hydroxylase (PHYH)- An enzyme involved in fatty acid α-oxidation. Phytanoyl-CoA is hydroxylated to 2-hydroxyphytanoyl-CoA. - Glyceronephosphate O-acyltransferase (GNPAT)- It is one of the initial enzymes used for synthesis of ether phospholipids. Dihydroxyacetone phosphate (DHAP) is acylated with acyl-CoA, forming acyl-DHAP. - Alkylglycerone phosphate synthase (AGPS)- In this reaction, the acyl group of acyl-DHAP is replaced by a long-chain fatty alcohol. The characteristic ether bond is formed and alkyl-DHAP is produced. - Fatty acyl-CoA reductase (FAR1/FAR2)- These are membrane-associated enzymes. Fatty acyl-CoA is reduced to supply the long-chain fatty alcohol required during ether lipid synthesis. - Alanine aminotransferase (AGT)- It is found in liver peroxisomes and takes part in glyoxylate metabolism. Glyoxylate is converted into glycine by this enzyme. ## Peroxisome Biogenesis Peroxisome biogenesis is the process of formation of new peroxisomes in a cell. They may arise by growth and division of already existing peroxisomes or by de novo formation from precursor membranes. Different proteins called peroxins (PEX proteins) are involved during this process. ![Peroxisome biogenesis diagram showing precursor membrane formation, PTS1 and PTS2 protein import through PEX proteins, receptor recycling, elongation, and DRP1-mediated division.](https://biologynotesonline.com/wp-content/uploads/2024/04/Peroxisome-Biogenesis-and-Protein-Import-Pathway-1024x768.webp)Peroxisome biogenesis diagram showing precursor membrane formation, PTS1 and PTS2 protein import through PEX proteins, receptor recycling, elongation, and DRP1-mediated division. Step 1- Peroxisomal membrane formation The first step includes formation and assembly of the peroxisomal membrane. Newly synthesized peroxisomal membrane proteins (PMPs) are recognized by PEX19 in the cytosol, which brings them to the membrane where PEX3 acts as its docking protein. PEX16 is also involved in membrane assembly and de novo biogenesis. Step 2- Formation of precursor vesicles During de novo formation, some membrane proteins are first sorted into specialized regions of the endoplasmic reticulum (ER). From these regions, small pre-peroxisomal vesicles (ppVs) are formed, which later join and develop into an import-competent peroxisome. In mammalian cells, precursor vesicles derived from mitochondria can also contribute in this process. Step 3- Synthesis of matrix proteins Peroxisomal matrix proteins are made on free ribosomes in the cytoplasm. These proteins possess specific peroxisomal targeting signals, mainly PTS1 or PTS2, which direct them towards the peroxisome. Step 4- Recognition of targeting signals The PTS1-containing protein is recognized by PEX5, while PEX7 recognizes PTS2 proteins. The receptor binds with its particular protein in the cytosol, forming a receptor-cargo complex. In mammals and plants, PEX7 also uses the long form of PEX5 (PEX5L) during PTS2 import. Step 5- Docking and matrix protein import The receptor-cargo complex now reaches the peroxisomal membrane. Here, docking takes place with PEX13 and PEX14. The cargo protein is then transported across the membrane and released into the peroxisomal matrix. Step 6- Recycling of PEX5 After releasing the cargo, PEX5 has to return back to the cytosol for another cycle. It gets monoubiquitinated and is removed from the peroxisomal membrane by the ATP-dependent PEX1-PEX6 complex. The RING peroxins PEX2, PEX10 and PEX12 participate in ubiquitination of the receptor. Step 7- Growth and division The mature peroxisome increases in size by addition of membrane components and proteins. Then membrane elongation takes place. In mammalian cells, PEX11β helps in this elongation and recruits the division machinery (MFF, FIS1 and DRP1). DRP1 finally constricts and splits the membrane, producing new peroxisomes. ## Functions of Peroxisomes - Fatty acid oxidation- The major role includes oxidation and metabolism of fatty acids. β-oxidation of very-long-chain fatty acids (VLCFAs) takes place here, along with the breakdown of branched-chain fatty acids. - Hydrogen peroxide metabolism- Production and degradation of hydrogen peroxide (H₂O₂). During oxidation reactions H₂O₂ is produced, which is broken down into water and oxygen by the enzyme catalase. - Ether lipid synthesis- The initial steps in formation of ether phospholipids, including plasmalogens, are carried out in peroxisomes. These are important components of nervous tissue and myelin. - Bile acid synthesis- In liver cells, formation of bile acids from cholesterol-derived intermediates also involves peroxisomes. - Photorespiration- Plant leaf peroxisomes take part in photorespiration, together with chloroplasts and mitochondria. - Glyoxylate cycle- Specialized peroxisomes of germinating oil-rich seeds participate in the glyoxylate cycle. Here, stored fatty acids are broken down and the products are used for conversion of stored lipids into carbohydrates. - Hormone synthesis- In plants, peroxisomes are also involved in formation of signaling molecules and plant hormones, including jasmonic acid (JA) and indole-3-acetic acid (IAA). - Detoxification- Oxidation of different harmful molecules and metabolites by peroxisomal enzymes, particularly in liver and kidney cells. ## Peroxisomes in Plant Cells Plant peroxisomes are highly dynamic organelles found in different plant tissues. Their enzyme content changes depending on the tissue and developmental condition of the plant. Photorespiration, fatty acid β-oxidation and utilization of stored lipids are some of the major activities. ![Photorespiration pathway showing glycolate, glycine, serine, and glycerate moving between chloroplasts, peroxisomes, and mitochondria.](https://biologynotesonline.com/wp-content/uploads/2024/04/Peroxisome-Role-in-Plant-Photorespiration-1024x576.webp)Photorespiration pathway showing glycolate, glycine, serine, and glycerate moving between chloroplasts, peroxisomes, and mitochondria. ### Photorespiration In plants, photorespiration takes place by the combined activity of [chloroplast](https://biologynotesonline.com/chloroplast/), peroxisome and mitochondrion. The compounds formed during the process move from one organelle to another. Chloroplast → Peroxisome → Mitochondrion → Peroxisome → Chloroplast The process is as follows- - In the chloroplast, RuBisCO undergoes oxygenation and forms 3-phosphoglycerate (3-PGA) and 2-phosphoglycolate (2-PG). This 2-PG is converted into glycolate. - Glycolate now moves into the peroxisome. Glycolate oxidase (GOX) oxidizes it to glyoxylate, producing hydrogen peroxide (H₂O₂) during the reaction. - The H₂O₂ is degraded into water and oxygen by catalase (CAT) present in the peroxisome. Glyoxylate is also converted to glycine by aminotransferase reaction. - Glycine enters into the mitochondrion where it forms serine. During this process CO₂ and ammonia are released. NADH is also produced. - The serine again comes back into the peroxisome. Here, serine and glyoxylate take part in formation of hydroxypyruvate, which is reduced to glycerate. - Glycerate is transported back to the chloroplast and converted into 3-phosphoglycerate (3-PGA). ### Fatty Acid Oxidation and Glyoxylate Cycle In plants, β-oxidation of fatty acids takes place in peroxisomes. It is highly active during germination of oil-storing seeds. Fatty acids are broken down repeatedly, producing acetyl-CoA and shorter fatty acyl molecules. The specialized peroxisomes present in germinating oil-rich seeds are historically known as glyoxysomes. They contain enzymes for fatty acid β-oxidation and also for the [glyoxylate cycle](https://biologynotesonline.com/the-glyoxylate-cycle/). A glyoxysome is a specialized peroxisome, whereas glyoxylate cycle is a metabolic pathway. During this pathway, acetyl-CoA obtained after fatty acid breakdown is used for formation of four-carbon compounds without the carbon-losing decarboxylation reactions of TCA cycle. These compounds enter into gluconeogenesis for formation of carbohydrates during germination. Stored lipid → Fatty acids → β-oxidation → Acetyl-CoA → Glyoxylate cycle → Four-carbon compounds → Carbohydrate formation ### Additional Plant Roles - Hormone metabolism- Peroxisomes are involved in plant hormone metabolism. In jasmonic acid (JA) formation, OPDA produced in chloroplast is transported into peroxisomes where further reactions including β-oxidation takes place. - Auxin metabolism- Conversion of indole-3-butyric acid (IBA) into indole-3-acetic acid (IAA), a process dependent on peroxisomes in plants such as Arabidopsis. - Plant development- They have roles in embryogenesis, seedling establishment and other developmental processes. Fatty acid β-oxidation is especially active during early seedling growth. - Environmental stress- Production and removal of reactive oxygen species (ROS), mainly H₂O₂. Their redox metabolism changes during heat, drought, high light and other environmental stresses. - Plant defense- Peroxisomes also participate in plant defense through ROS metabolism and hormone pathways, particularly the jasmonate-associated responses. ## Mechanisms of Peroxisomes ### Fatty Acid Oxidation by Peroxisome Fatty acid oxidation in peroxisomes takes place by the β-oxidation pathway. In mammalian cells, very-long-chain fatty acids (VLCFAs) are important substrates. With each cycle, the fatty acyl chain becomes shorter by two carbon atoms. ![Peroxisomal beta-oxidation pathway showing VLCFA transport, ACOX, DBP and thiolase reactions, hydrogen peroxide formation, and progressive fatty-acid chain shortening.](https://biologynotesonline.com/wp-content/uploads/2024/04/Peroxisomal-Beta-Oxidation-of-Very-Long-Chain-Fatty-Acids-1024x576.webp)Peroxisomal beta-oxidation pathway showing VLCFA transport, ACOX, DBP and thiolase reactions, hydrogen peroxide formation, and progressive fatty-acid chain shortening. The process takes place in the following steps- - Fatty acid is first activated to fatty acyl-CoA in presence of ATP. Enzyme involved- Acyl-CoA synthetase. - This fatty acyl-CoA is then transported into the peroxisome. ABCD1, ABCD2 and ABCD3 transporters present in peroxisomal membrane are involved in transport of different β-oxidation substrates. - Fatty acyl-CoA is oxidised to trans-2-enoyl-CoA. During this step, hydrogen peroxide (H₂O₂) is formed which is broken down by catalase. Enzyme involved- Acyl-CoA oxidase (ACOX). - The trans-2-enoyl-CoA now takes up water and forms 3-hydroxyacyl-CoA. In mammals, this reaction is carried out by D-bifunctional protein (DBP/MFE2). - In the next reaction, 3-hydroxyacyl-CoA is oxidised into 3-ketoacyl-CoA, NAD⁺ is reduced to NADH. Enzyme involved- D-bifunctional protein (DBP/MFE2). - 3-ketoacyl-CoA is cleaved in presence of CoA-SH, producing acetyl-CoA and a fatty acyl-CoA which is shorter by two carbon atoms. Enzyme involved- Peroxisomal thiolase. - This shortened fatty acyl-CoA again enters into the same β-oxidation reactions. Two carbon atoms are removed in every cycle. - The shortened fatty acyl products and acetyl-CoA are transferred out from the peroxisome. Further oxidation can take place in the mitochondria, as peroxisomes do not contain [citric acid cycle](https://biologynotesonline.com/krebs-cycle/) and respiratory chain. ### Hydrogen Peroxide and Redox Metabolism Peroxisomes are involved in both the production and removal of hydrogen peroxide (H₂O₂). Thus, peroxisomes do not merely destroy H₂O₂, its formation is also a normal part of peroxisomal metabolism. ![Peroxisomal redox diagram showing hydrogen peroxide production by oxidative reactions, removal by catalase and antioxidant systems, redox signaling, and oxidative damage when peroxide accumulates.](https://biologynotesonline.com/wp-content/uploads/2024/04/Hydrogen-Peroxide-Metabolism-in-Peroxisomes-1024x768.webp)Peroxisomal redox diagram showing hydrogen peroxide production by oxidative reactions, removal by catalase and antioxidant systems, redox signaling, and oxidative damage when peroxide accumulates. - Different oxidative reactions taking place in peroxisomes transfer electrons to molecular oxygen. During fatty acid oxidation and several other reactions, H₂O₂ is produced as one of the products. - The hydrogen peroxide formed is kept under control mainly by catalase, one of the abundant enzymes of peroxisomes. It converts H₂O₂ into water and oxygen.The reaction is as follows-2 H₂O₂ → 2 H₂O + O₂ - Other antioxidant systems are also present along with catalase. Peroxiredoxins, glutathione peroxidase and glutathione-associated systems can take part in controlling peroxisomal ROS, depending upon the organism and cell. - Not all H₂O₂ has only a harmful role. When present in controlled amount, peroxisome-derived H₂O₂ can act as a redox signaling molecule, affecting redox-sensitive proteins and different cellular signaling processes. - When its production goes beyond the antioxidant capacity, H₂O₂ and other [reactive oxygen species (ROS)](https://biologynotesonline.com/reactive-oxygen-species-ros-definition-types-chemistry-defence-roles/) accumulate. Oxidation of proteins, membrane lipids and other cellular components can then occur. - Therefore, the peroxisomal redox system involves a balance between oxidative reactions → H₂O₂ generation → catalase/antioxidant control. ### Ether Lipid and Plasmalogen Synthesis Ether phospholipid synthesis starts in peroxisomes and the remaining part takes place in the [endoplasmic reticulum (ER)](https://biologynotesonline.com/endoplasmic-reticulum/). Plasmalogens are one of the major ether phospholipids, having a vinyl-ether bond. ![Ether lipid synthesis pathway showing DHAP conversion in the peroxisome, FAR1/FAR2 and AGPS reactions, transfer of the ether-lipid precursor to the ER, and formation of plasmalogens.](https://biologynotesonline.com/wp-content/uploads/2024/04/Peroxisomal-Ether-Lipid-and-Plasmalogen-Synthesis-1024x576.webp)Ether lipid synthesis pathway showing DHAP conversion in the peroxisome, FAR1/FAR2 and AGPS reactions, transfer of the ether-lipid precursor to the ER, and formation of plasmalogens. - In the first step, dihydroxyacetone phosphate (DHAP) is acylated by long-chain acyl-CoA and acyl-DHAP is formed. Enzyme involved- Glyceronephosphate O-acyltransferase (GNPAT). - This acyl-DHAP is then changed into alkyl-DHAP. Here, the acyl group is replaced by a long-chain fatty alcohol, forming the ether bond. Enzyme involved- Alkylglycerone phosphate synthase (AGPS). - The long-chain fatty alcohol required in this reaction is supplied mainly by FAR1 and FAR2, present in the peroxisomal membrane. Fatty acyl-CoA is reduced by these enzymes. - Alkyl-DHAP is further reduced and 1-O-alkyl-glycerol-3-phosphate (alkyl-G3P) is formed. This ether lipid precursor now moves to the ER. - In the ER, the next reactions take place. Second fatty-acyl chain and polar head group are added. The vinyl double bond present in plasmalogens is also formed here. - Plasmalogens are found in high amount in nervous tissue, especially the myelin sheath. An important phospholipid component of these membranes. - In nervous-system membranes, they take part in membrane organization and membrane dynamics. Deficiency of plasmalogens is associated with abnormalities of myelin and nervous-system function. ## Cooperation With Other Organelles Peroxisomes have interactions with mitochondria, endoplasmic reticulum (ER) and lipid droplets during different cellular metabolisms. Fatty acids and lipid materials are passed in between these organelles. - Mitochondria- Both peroxisomes and mitochondria are involved in fatty acid metabolism. In mammals, very-long-chain fatty acids (VLCFAs) are first shortened in peroxisomes, the products formed are then passed on to [mitochondria](https://biologynotesonline.com/mitochondria/) where further oxidation takes place. As these metabolisms occur, production and removal of reactive oxygen species (ROS) also take place in both organelles, involved in cellular redox balance. - Endoplasmic reticulum (ER)- It supplies phospholipids needed for growth of the peroxisomal membrane. The synthesis of ether phospholipids is shared between these two organelles. Early reactions occur in peroxisomes. The later part is carried out in ER. - Lipid droplets- These are storage sites of neutral lipids, from which fatty acids are released and transferred to peroxisomes for β-oxidation. Peroxisomes also form contacts with lipid droplets during this movement of fatty acids. ## Peroxisomal Disorders Peroxisomal disorders are inherited metabolic diseases produced by defects in formation of peroxisomes or in a particular peroxisomal protein. The following are some of the important peroxisomal disorders- - Zellweger spectrum disorder (ZSD)- It is a group of peroxisome biogenesis disorders caused by defects in PEX genes. Peroxisomal assembly and several metabolic activities are affected together. Severe forms show neurological abnormalities, liver disease, hearing and visual defects. - X-linked adrenoleukodystrophy (X-ALD)- This disorder results from mutation of the ABCD1 gene, coding for a peroxisomal membrane transporter. Transport and β-oxidation of very-long-chain fatty acids (VLCFAs) are affected and VLCFAs accumulate in tissues. Nervous system and adrenal cortex are commonly involved. - Rhizomelic chondrodysplasia punctata (RCDP)- A disorder mainly associated with defective plasmalogen synthesis. RCDP type 1 occurs due to PEX7 defect, whereas other forms can result from defects of enzymes taking part in plasmalogen formation. Shortening of proximal limbs, skeletal abnormalities, cataracts and developmental defects are characteristic features. - D-bifunctional protein deficiency- The HSD17B4 gene is affected in this disorder. Peroxisomal β-oxidation becomes defective. Neonatal hypotonia, seizures and severe developmental abnormalities are commonly seen. - Acyl-CoA oxidase 1 deficiency- It is caused by deficiency of ACOX1, an enzyme participating in peroxisomal fatty acid β-oxidation. VLCFAs accumulate. The affected individuals may show hypotonia, seizures, developmental delay, hearing loss and later neurological deterioration. - Adult Refsum disease- Breakdown of phytanic acid by peroxisomal α-oxidation is affected, most commonly due to mutation in PHYH and sometimes PEX7. Phytanic acid therefore accumulates in tissues and body fluids. Retinitis pigmentosa, loss of smell, peripheral neuropathy and ataxia are some of the major features. ## References - Agrawal, G., & Subramani, S. (2016). De novo peroxisome biogenesis: Evolving concepts and conundrums. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1863(5), 892–901. [https://doi.org/10.1016/j.bbamcr.2015.09.014](https://doi.org/10.1016/j.bbamcr.2015.09.014) - Alberts, B., Johnson, A., Lewis, J., Raff, M., Roberts, K., & Walter, P. (2002). Peroxisomes. In Molecular biology of the cell (4th ed.). Garland Science. [https://www.ncbi.nlm.nih.gov/books/NBK26858/](https://www.ncbi.nlm.nih.gov/books/NBK26858/) - Argyriou, C., D’Agostino, M. D., & Braverman, N. (2016). Peroxisome biogenesis disorders. Translational Science of Rare Diseases, 1(2), 111–144. [https://doi.org/10.3233/TRD-160003](https://doi.org/10.3233/TRD-160003) - Bozelli, J. C., Jr., & Epand, R. M. (2021). Plasmalogen replacement therapy. Membranes, 11(11), 838. [https://doi.org/10.3390/membranes11110838](https://doi.org/10.3390/membranes11110838) - Chornyi, S., Ofman, R., Koster, J., & Waterham, H. R. (2023). The origin of long-chain fatty acids required for de novo ether lipid/plasmalogen synthesis. Journal of Lipid Research, 64(5), 100364. [https://doi.org/10.1016/j.jlr.2023.100364](https://doi.org/10.1016/j.jlr.2023.100364) - Cooper, G. M. (2000). Peroxisomes. In The cell: A molecular approach (2nd ed.). Sinauer Associates. [https://www.ncbi.nlm.nih.gov/books/NBK9930/](https://www.ncbi.nlm.nih.gov/books/NBK9930/) - Dellero, Y., Jossier, M., Schmitz, J., Maurino, V. G., & Hodges, M. (2016). Photorespiratory glycolate–glyoxylate metabolism. Journal of Experimental Botany, 67(10), 3041–3052. [https://doi.org/10.1093/jxb/erw090](https://doi.org/10.1093/jxb/erw090) - Dorninger, F., Forss-Petter, S., & Berger, J. (2017). From peroxisomal disorders to common neurodegenerative diseases: The role of ether phospholipids in the nervous system. FEBS Letters, 591(18), 2761–2788. [https://doi.org/10.1002/1873-3468.12788](https://doi.org/10.1002/1873-3468.12788) - Fransen, M., Lismont, C., & Walton, P. (2017). The peroxisome-mitochondria connection: How and why? International Journal of Molecular Sciences, 18(6), 1126. [https://doi.org/10.3390/ijms18061126](https://doi.org/10.3390/ijms18061126) - Frick, E. M., & Strader, L. C. (2018). Roles for IBA-derived auxin in plant development. Journal of Experimental Botany, 69(2), 169–177. [https://doi.org/10.1093/jxb/erx298](https://doi.org/10.1093/jxb/erx298) - Gabaldón, T. (2010). Peroxisome diversity and evolution. Philosophical Transactions of the Royal Society B: Biological Sciences, 365(1541), 765–773. [https://doi.org/10.1098/rstb.2009.0240](https://doi.org/10.1098/rstb.2009.0240) - Hasan, S., Platta, H. W., & Erdmann, R. (2013). Import of proteins into the peroxisomal matrix. Frontiers in Physiology, 4, 261. [https://doi.org/10.3389/fphys.2013.00261](https://doi.org/10.3389/fphys.2013.00261) - He, A., Dean, J. M., & Lodhi, I. J. (2021). Peroxisomes as cellular adaptors to metabolic and environmental stress. Trends in Cell Biology, 31(8), 656–670. [https://doi.org/10.1016/j.tcb.2021.02.005](https://doi.org/10.1016/j.tcb.2021.02.005) - Hu, J., Baker, A., Bartel, B., Linka, N., Mullen, R. T., Reumann, S., & Zolman, B. K. (2012). Plant peroxisomes: Biogenesis and function. The Plant Cell, 24(6), 2279–2303. [https://doi.org/10.1105/tpc.112.096586](https://doi.org/10.1105/tpc.112.096586) - Huang, H., Liu, B., Liu, L., & Song, S. (2017). Jasmonate action in plant growth and development. Journal of Experimental Botany, 68(6), 1349–1359. [https://doi.org/10.1093/jxb/erw495](https://doi.org/10.1093/jxb/erw495) - Kao, Y.-T., Gonzalez, K. L., & Bartel, B. (2018). Peroxisome function, biogenesis, and dynamics in plants. Plant Physiology, 176(1), 162–177. [https://doi.org/10.1104/pp.17.01050](https://doi.org/10.1104/pp.17.01050) - Kaur, N., Reumann, S., & Hu, J. (2009). Peroxisome biogenesis and function. The Arabidopsis Book, 7, e0123. [https://doi.org/10.1199/tab.0123](https://doi.org/10.1199/tab.0123) - Kumar, R., Islinger, M., Worthy, H., Carmichael, R., & Schrader, M. (2024). The peroxisome: An update on mysteries 3.0. Histochemistry and Cell Biology, 161(2), 99–132. [https://doi.org/10.1007/s00418-023-02259-5](https://doi.org/10.1007/s00418-023-02259-5) - Le, X. H., & Millar, A. H. (2023). The diversity of substrates for plant respiration and how to optimize their use. Plant Physiology, 191(4), 2133–2149. [https://doi.org/10.1093/plphys/kiac599](https://doi.org/10.1093/plphys/kiac599) - Lismont, C., Revenco, I., & Fransen, M. (2019). Peroxisomal hydrogen peroxide metabolism and signaling in health and disease. International Journal of Molecular Sciences, 20(15), 3673. [https://doi.org/10.3390/ijms20153673](https://doi.org/10.3390/ijms20153673) - Lodhi, I. J., & Semenkovich, C. F. (2014). Peroxisomes: A nexus for lipid metabolism and cellular signaling. Cell Metabolism, 19(3), 380–392. [https://doi.org/10.1016/j.cmet.2014.01.002](https://doi.org/10.1016/j.cmet.2014.01.002) - Ma, C., Agrawal, G., & Subramani, S. (2011). Peroxisome assembly: Matrix and membrane protein biogenesis. Journal of Cell Biology, 193(1), 7–16. [https://doi.org/10.1083/jcb.201010022](https://doi.org/10.1083/jcb.201010022) - Pan, R., Liu, J., & Hu, J. (2019). Peroxisomes in plant reproduction and seed-related development. Journal of Integrative Plant Biology, 61(7), 784–802. [https://doi.org/10.1111/jipb.12765](https://doi.org/10.1111/jipb.12765) - Raychaudhuri, S., & Prinz, W. A. (2008). Nonvesicular phospholipid transfer between peroxisomes and the endoplasmic reticulum. Proceedings of the National Academy of Sciences of the United States of America, 105(41), 15785–15790. [https://doi.org/10.1073/pnas.0808321105](https://doi.org/10.1073/pnas.0808321105) - Sandalio, L. M., Peláez-Vico, M. A., Molina-Moya, E., & Romero-Puertas, M. C. (2021). Peroxisomes as redox-signaling nodes in intracellular communication and stress responses. Plant Physiology, 186(1), 22–35. [https://doi.org/10.1093/plphys/kiab060](https://doi.org/10.1093/plphys/kiab060) - Schrader, M., Kamoshita, M., & Islinger, M. (2020). Organelle interplay: Peroxisome interactions in health and disease. Journal of Inherited Metabolic Disease, 43(1), 71–89. [https://doi.org/10.1002/jimd.12083](https://doi.org/10.1002/jimd.12083) - Shimada, T. L., Hayashi, M., & Hara-Nishimura, I. (2018). Membrane dynamics and multiple functions of oil bodies in seeds and leaves. Plant Physiology, 176(1), 199–207. [https://doi.org/10.1104/pp.17.01522](https://doi.org/10.1104/pp.17.01522) - Smith, J. J., & Aitchison, J. D. (2013). Peroxisomes take shape. Nature Reviews Molecular Cell Biology, 14(12), 803–817. [https://doi.org/10.1038/nrm3700](https://doi.org/10.1038/nrm3700) - Sparkes, I. A., & Baker, A. (2002). Peroxisome biogenesis and protein import in plants, animals and yeasts: Enigma and variations? Molecular Membrane Biology, 19(3), 171–185. [https://doi.org/10.1080/09687680210159422](https://doi.org/10.1080/09687680210159422) - Sundaram, S. S., Bove, K. E., Lovell, M. A., & Sokol, R. J. (2008). Mechanisms of disease: Inborn errors of bile acid synthesis. Nature Clinical Practice Gastroenterology & Hepatology, 5(8), 456–468. [https://doi.org/10.1038/ncpgasthep1179](https://doi.org/10.1038/ncpgasthep1179) - Tawbeh, A., Gondcaille, C., Trompier, D., & Savary, S. (2021). Peroxisomal ABC transporters: An update. International Journal of Molecular Sciences, 22(11), 6093. [https://doi.org/10.3390/ijms22116093](https://doi.org/10.3390/ijms22116093) - Terlecky, S. R., Koepke, J. I., & Walton, P. A. (2006). Peroxisomes and aging. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1763(12), 1749–1754. [https://doi.org/10.1016/j.bbamcr.2006.08.017](https://doi.org/10.1016/j.bbamcr.2006.08.017) - Turk, B. R., Theda, C., Fatemi, A., & Moser, A. B. (2020). X-linked adrenoleukodystrophy: Pathology, pathophysiology, diagnostic testing, newborn screening and therapies. International Journal of Developmental Neuroscience, 80(1), 52–72. [https://doi.org/10.1002/jdn.10003](https://doi.org/10.1002/jdn.10003) - van den Brink, D. M., Brites, P., Haasjes, J., Wierzbicki, A. S., Mitchell, J., Lambert-Hamill, M., de Belleroche, J., Jansen, G. A., Waterham, H. R., & Wanders, R. J. A. (2003). Identification of PEX7 as the second gene involved in Refsum disease. American Journal of Human Genetics, 72(2), 471–477. [https://doi.org/10.1086/346093](https://doi.org/10.1086/346093) - van den Brink, D. M., & Wanders, R. J. A. (2006). Phytanic acid: Production from phytol, its breakdown and role in human disease. Cellular and Molecular Life Sciences, 63(15), 1752–1765. [https://doi.org/10.1007/s00018-005-5463-y](https://doi.org/10.1007/s00018-005-5463-y) - Vasko, R. (2016). Peroxisomes and kidney injury. Antioxidants & Redox Signaling, 25(4), 217–231. [https://doi.org/10.1089/ars.2016.6666](https://doi.org/10.1089/ars.2016.6666) - Vaz, F. M., Ferdinandusse, S., Salomons, G. S., & Wanders, R. J. A. (2025). Disorders of fatty acid homeostasis. Journal of Inherited Metabolic Disease, 48(1), e12734. [https://doi.org/10.1002/jimd.12734](https://doi.org/10.1002/jimd.12734) - Walker, C. L., Pomatto, L. C. D., Tripathi, D. N., & Davies, K. J. A. (2018). Redox regulation of homeostasis and proteostasis in peroxisomes. Physiological Reviews, 98(1), 89–115. [https://doi.org/10.1152/physrev.00033.2016](https://doi.org/10.1152/physrev.00033.2016) - Wanders, R. J. A., Vaz, F. M., Waterham, H. R., & Ferdinandusse, S. (2020). Fatty acid oxidation in peroxisomes: Enzymology, metabolic crosstalk with other organelles and peroxisomal disorders. Advances in Experimental Medicine and Biology, 1299, 55–70. [https://doi.org/10.1007/978-3-030-60204-8_5](https://doi.org/10.1007/978-3-030-60204-8_5) - Wanders, R. J. A., Waterham, H. R., & Ferdinandusse, S. (2016). Metabolic interplay between peroxisomes and other subcellular organelles including mitochondria and the endoplasmic reticulum. Frontiers in Cell and Developmental Biology, 3, 83. [https://doi.org/10.3389/fcell.2015.00083](https://doi.org/10.3389/fcell.2015.00083) - Wang, X., Li, S., Liu, Y., & Ma, C. (2015). Redox regulated peroxisome homeostasis. Redox Biology, 4, 104–108. [https://doi.org/10.1016/j.redox.2014.12.006](https://doi.org/10.1016/j.redox.2014.12.006)