Peroxidase, molecular formula NULL, CAS 9003-99-0, It is a marker enzyme of peroxisomes and a type of oxidoreductase that can catalyze many reactions. Peroxidas is an enzyme that catalyzes substrate oxidation using hydrogen peroxide as an electron acceptor. It mainly exists in the peroxisomes of the carrier, with iron porphyrin as a secondary group, which can catalyze hydrogen peroxide, oxidize phenolic and amine compounds, and hydrocarbon oxidation products, and has a dual effect of eliminating the toxicity of hydrogen peroxide and phenolic, amine, aldehyde, and benzene compounds. Peroxidas is a type of oxidoreductase. Distributed in body fluids or cells such as milk, white blood cells, and platelets, this enzyme also has heme as its cofactor. It catalyzes the oxidation of substrates using H2O2 as an electron acceptor. It catalyzes the direct oxidation of phenolic or amine compounds by H2O2, such as glutathione peroxidas, eosinophil peroxidas, and thyroid peroxidas, and has a dual effect on eliminating the toxicity of hydrogen peroxide and phenolic amines. The reaction is as follows: R+H2O2RO+H2O or RH2+H2O2-R+2H2O. In clinical diagnosis, observing the presence of occult blood in feces is to utilize the activity of peroxidas in red blood cells to oxidize aniline into blue compounds.
Medium enzyme
(1) Animals
Peroxisomes are involved in the beta oxidation of fatty acids in animals (another organelle is mitochondria), and the concentration of peroxisomes in rat liver cells increased tenfold after taking Jiangzhi Ling. In addition, peroxisomes also have detoxifying effects, as catalse can use H2O2 to oxidize harmful substances such as phenols, formaldehyde, formic acid, and alcohols. One fourth of the ingested alcohol is oxidized to acetaldehyde in peroxisomes.
(2) Plants
In plants, peroxisomes mainly include:
① Participate in photorespiration and oxidize the byproduct of photosynthesis, glycolic acid, to acetaldehyde and hydrogen peroxide.
② In germinating seeds, β - oxidation of fat occurs to produce acetyl CoA, which is broken down by isocitrate into acetic acid and succinic acid through the glyoxylate cycle. It is then added to the tricarboxylic acid cycle, also known as the glyoxysome, as it involves the glyoxylate cycle.
Functional response
The function of peroxidase:
This function is achieved by catalse using hydrogen peroxide to oxidize various substrates such as phenol, formic acid, formaldehyde, and ethanol. The oxidation results in these toxic substances becoming non-toxic, effectively decomposing formaldehyde and toluene. At the same time, it also further converts H2O2 into non-toxic H2O. This detoxification effect is particularly important for the liver and kidneys. For example, almost half of the ethanol people drink is oxidized to acetaldehyde in this way, thereby relieving the toxic effects of ethanol on cells.
The sensitivity of peroxisomes and mitochondria to oxygen is different. The optimal oxygen concentration required for mitochondrial oxidation is around 2%. Increasing the oxygen concentration does not improve the oxidative capacity of mitochondria. The oxidation rate of peroxisomes increases proportionally with the increase of oxygen tension. Therefore, under low concentration oxygen conditions, mitochondria have a stronger ability to utilize oxygen than peroxisomes. However, in high concentration oxygen conditions, the oxidative reaction of peroxisomes dominates, which gives peroxisomes the ability to protect cells from the toxicity of high concentration oxygen.
Approximately 25-50% of fatty acids in animal tissues are oxidized in peroxisomes, while the rest are oxidized in mitochondria. In addition, due to the presence of enzymes related to phospholipid synthesis in peroxisomes, peroxisomes also participate in lipid synthesis.
In most animal cells, urate oxidase is essential for the oxidation of uric acid. Uric acid is a product of the degradation metabolism of nucleotides and certain proteins, and uric acid oxidase can further oxidize and remove this metabolic waste. In addition, peroxisomes are also involved in other nitrogen metabolism, such as transaminase catalyzing the transfer of amino groups.
Reaction of peroxisomes:
The commonality of various oxidases is that they oxidize substrates to generate hydrogen peroxide.
RH2+O2→R+H2O2
Catalse can also use hydrogen peroxide to oxidize other substrates such as aldehydes, alcohols, and phenols.
R′H2+H2O2→R′+2H2O
In addition, when there is an excess of H2O2 in the cell, catalse can also catalyze the following reactions:
2H2O2 → 2H2O + O2
Enzyme body:
Peroxisomes are vesicles enclosed by a unit membrane, with a diameter of approximately 0.5-1.0 μ m, typically smaller than mitochondria. Commonly present in various cells of eukaryotes, with particularly high numbers in liver and kidney cells. The hallmark enzyme of peroxisomes is catalse, which mainly hydrolyzes hydrogen peroxide. Hydrogen peroxide (H2O2) is a cytotoxic substance produced in the oxidation-reduction reaction catalyzed by oxidase. Both oxidase and catalse are present in the peroxisome, providing protection to cells.
Plants contain a large number of peroxisomes, which are highly active enzymes. It is related to respiration, photosynthesis, and oxidation of auxin. During the process of plant growth and development, its activity constantly changes. The activity is generally higher in aged tissues and weaker in young tissues. This is because peroxidase can convert certain carbohydrates contained in tissues into lignin, increasing the degree of lignification. Moreover, it has been found that the activity of peroxidas increases in rice roots with premature aging and reduced yield. Therefore, peroxidas can be used as a physiological indicator of tissue aging. In addition, the important role of peroxidas isoenzymes in genetic breeding is also receiving attention.
Guaiacolase is a type of oxidoreductase widely present in animals, plants, and microorganisms. Its development history can be summarized according to the timeline as follows:
Scientists began to pay attention to substances with redox activity inside cells, but the specific form of guaiacolase was not yet clear. Early research mainly focused on the oxidase activity in plant tissues, and found that certain plant extracts could catalyze the decomposition of hydrogen peroxide.
With the deepening of enzymatic research, scientists gradually isolated proteins with guaiacolase activity. In 1928, Keilin and Hartree first isolated horseradish guaiacolase (HRP) from horseradish and systematically studied its catalytic properties, laying the foundation for subsequent guaiacolase research.
Research revealed the core role of guaiacolase in biological metabolism, including participation in lignin synthesis, defense against pathogen invasion, and regulation of redox balance. In 1954, J. Rhodin discovered a monolayer membrane wrapped organelle in mouse renal tubular epithelial cells, which was later named peroxisomes, further clarifying the cellular localization of peroxidase.
Through biochemical and molecular biology techniques, scientists elucidated the catalytic mechanism of guaiacolase and discovered that it uses heme as a secondary group to catalyze the decomposition of hydrogen peroxide through the redox cycle of the iron porphyrin ring. Meanwhile, the study revealed the key role of peroxisomes in fatty acid beta oxidation, bile acid synthesis, and regulation of reactive oxygen species metabolism.
With the rise of genetic engineering technology, scientists successfully cloned and expressed various guaiacolase genes, such as glutathione guaiacolase and thyroid guaiacolase, which promoted their application in medical diagnosis and treatment. For example, HRP has become a core tool for immunohistochemical staining and serum anti nuclear antibody detection due to its high stability.
Research has revealed that peroxisome dysfunction is closely related to various diseases, such as Zellweger syndrome, inherited diseases such as adrenal leukodystrophy, as well as complex diseases such as cancer and neurodegenerative diseases. For example, peroxisome defects lead to the accumulation of reactive oxygen species, causing cell damage and inflammatory reactions.
With the development of single-cell sequencing and spatial omics technology, scientists discovered the core role of peroxisomes in cell type specific metabolic regulation. For example, a 2025 study in Science revealed that macrophage peroxisomes inhibit chronic fibrosis after viral lung injury by regulating mitochondrial homeostasis, providing a new target for the treatment of COVID-19 sequelae.
Future direction and technological innovation
Synthetic Biology and Metabolic Engineering: By modifying the peroxisome metabolic pathway, the biosynthesis of high-value compounds (such as polyhydroxyalkanoates) can be achieved, promoting green manufacturing and sustainable development.
Precision medicine and drug development: Based on the regulation mechanism of peroxisome function, develop new therapies for metabolic diseases, neurodegenerative diseases, and viral infections, such as promoting peroxisome biogenesis through small molecule drugs to improve tissue repair ability.
faq
What is the function of peroxidase?
Peroxidases are a group of enzymes that catalyze the oxidation of a substrate by hydrogen peroxide or an organic peroxide. Most peroxidases are ferric heme proteins – one notable exception being the glutathione peroxidase, which is a selenium-containing enzyme.
What does high peroxidase mean?
Thyroid peroxidase (TPO) antibodies
If you test positive for TPO antibodies (have a high amount) it may mean: You have Hashimoto's disease (if you have high TSH levels) You may develop hypothyroidism later in life (if your TSH levels are currently normal or near normal)
What is a peroxidase test for?
Doctors order thyroid peroxidase antibodies tests: to diagnose and monitor autoimmune conditions involving the thyroid, such as Hashimoto's thyroiditis and Graves' disease. to diagnose thyroid disorders such as thyroiditis (inflammation of the thyroid) or goiter (an enlarged thyroid)
What is the difference between catalase and peroxidase?
Both enzymes use one molecule of hydrogen peroxide to form a high valent iron intermediate named Compound I (Cpd I). However, whereas catalase Cpd I oxidizes a second H2O2 molecule to oxygen, peroxidases use this intermediate to oxidize other substrates rather than H2O2.
What is another name for peroxidase?
Peroxidases or peroxide reductases (EC number 1.11. 1. x) are a large group of enzymes which play a role in various biological processes. They are named after the fact that they commonly break up peroxides, and should not be confused with other enzymes that produce peroxide, which are often oxidases.
Is peroxidase used in Elisa?
Horseradish peroxidase is commonly used in various diagnostic tests and assays in the fields of immunology and molecular biology. Enzyme-linked immunosorbent assay (ELISA): HRP is used as a detection enzyme in ELISA, a test that detects the presence of antibodies or antigens in a sample.
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