Chloride Peroxidase
Peroxidases
Horseradish Peroxidase
Glutathione Peroxidase
Peroxidase
Cytochrome-c Peroxidase
Chloride Channels
Ascorbate Peroxidases
Eosinophil Peroxidase
Iodide Peroxidase
Vinyl Chloride
Polyvinyl Chloride
Hydrogen Peroxide
Guaiacol
Catalase
Mercuric Chloride
Selenium
Heterologous expression of the vanadium-containing chloroperoxidase from Curvularia inaequalis in Saccharomyces cerevisiae and site-directed mutagenesis of the active site residues His(496), Lys(353), Arg(360), and Arg(490). (1/107)
The vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis is heterologously expressed to high levels in the yeast Saccharomyces cerevisiae. Characterization of the recombinant enzyme reveals that this behaves very similar to the native chloroperoxidase. Site-directed mutagenesis is performed on four highly conserved active site residues to examine their role in catalysis. When the vanadate-binding residue His(496) is changed into an alanine, the mutant enzyme loses the ability to bind vanadate covalently resulting in an inactive enzyme. The negative charges on the vanadate oxygens are compensated by hydrogen bonds with the residues Arg(360), Arg(490), and Lys(353). When these residues are changed into alanines the mutant enzymes lose the ability to effectively oxidize chloride but can still function as bromoperoxidases. A general mechanism for haloperoxidase catalysis is proposed that also correlates the kinetic properties of the mutants with the charge and the hydrogen-bonding network in the vanadate-binding site. (+info)Striking activation of oxidative enzymes suspended in nonaqueous media. (2/107)
The catalytic activity of four lyophilized oxidative enzymes-horseradish peroxidase, soybean peroxidase, Caldariomyces fumago chloroperoxidase, and mushroom polyphenol oxidase-is much lower when directly suspended in organic solvents containing little water than when they are introduced into the same largely nonaqueous media by first dissolving them in water and then diluting with anhydrous solvents. The lower the water content of the medium, the greater this discrepancy becomes. The mechanism of this phenomenon was found to arise from reversible denaturation of the oxidases on lyophilization: because of its conformational rigidity, the denatured enzyme exhibits very limited activity when directly suspended in largely nonaqueous media but renatures and thus yields much higher activity if first redissolved in water. Two independent means were discovered for dramatically minimizing the lyophilization-induced inactivation, both involving the addition of certain types of excipients to the aqueous enzyme solution before lyophilization. The first group of excipients consists of phenolic and aniline substrates as well as other hydrophobic compounds; these presumably bind to the hydrophobic pocket of the enzyme active site, thereby preventing its collapse during dehydration. The second group consists of general lyoprotectants such as polyols and polyethylen glycol that apparently preserve the overall enzyme structure during dehydration. The activation effects of such excipients can reach into the tens and hundreds of fold. Moreover, the activations afforded by the two excipient groups are additive, resulting in up to a complete protection against lyophilization-induced inactivation when representatives of the two are present together. (+info)Replacement of the proximal heme thiolate ligand in chloroperoxidase with a histidine residue. (3/107)
Chloroperoxidase is a versatile heme enzyme which can cross over the catalytic boundaries of other oxidative hemoproteins and perform multiple functions. Chloroperoxidase, in addition to catalyzing classical peroxidative reactions, also acts as a P450 cytochrome and a potent catalase. The multiple functions of chloroperoxidase must be derived from its unique active site structure. Chloroperoxidase possesses a proximal cysteine thiolate heme iron ligand analogous to the P450 cytochromes; however, unlike the P450 enzymes, chloroperoxidase possesses a very polar environment distal to its heme prosthetic group and contains a glutamic acid residue in close proximity to the heme iron. The presence of a thiolate ligand in chloroperoxidase has long been thought to play an essential role in its chlorination and epoxidation activities; however, the research reported in this paper proves that hypothesis to be invalid. To explore the role of Cys-29, the amino acid residue supplying the thiolate ligand in chloroperoxidase, Cys-29 has been replaced with a histidine residue. Mutant clones of the chloroperoxidase genome have been expressed in a Caldariomyces fumago expression system by using gene replacement rather than gene insertion technology. C. fumago produces wild-type chloroperoxidase, thus requiring gene replacement of the wild type by the mutant gene. To the best of our knowledge, this is the first time that gene replacement has been reported for this type of fungus. The recombinant histidine mutants retain most of their chlorination, peroxidation, epoxidation, and catalase activities. These results downplay the importance of a thiolate ligand in chloroperoxidase and suggest that the distal environment of the heme active site plays the major role in maintaining the diverse activities of this enzyme. (+info)Peroxidase and phosphatase activity of active-site mutants of vanadium chloroperoxidase from the fungus Curvularia inaequalis. Implications for the catalytic mechanisms. (4/107)
Mutation studies were performed on active-site residues of vanadium chloroperoxidase from the fungus Curvularia inaequalis, an enzyme which exhibits both haloperoxidase and phosphatase activity and is related to glucose-6-phosphatase. The effects of mutation to alanine on haloperoxidase activity were studied for the proposed catalytic residue His-404 and for residue Asp-292, which is located close to the vanadate cofactor. The mutants were strongly impaired in their ability to oxidize chloride but still oxidized bromide, although they inactivate during turnover. The effects on the optical absorption spectrum of vanadium chloroperoxidase indicate that mutant H404A has a reduced affinity for the cofactor, whereas this affinity is unchanged in mutant D292A. The effect on the phosphatase activity of the apoenzyme was investigated for six mutants of putative catalytic residues. Effects of mutation of His-496, Arg-490, Arg-360, Lys-353, and His-404 to alanine are in line with their proposed roles in nucleophilic attack, transition-state stabilization, and leaving-group protonation. Asp-292 is excluded as the group that protonates the leaving group. A model based on the mutagenesis studies is presented and may serve as a template for glucose-6-phosphatase and other related phosphatases. Hydrolysis of a phospho-histidine intermediate is the rate-determining step in the phosphatase activity of apochloroperoxidase, as shown by burst kinetics. (+info)X-ray structures of a novel acid phosphatase from Escherichia blattae and its complex with the transition-state analog molybdate. (5/107)
The structure of Escherichia blattae non-specific acid phosphatase (EB-NSAP) has been determined at 1.9 A resolution with a bound sulfate marking the phosphate-binding site. The enzyme is a 150 kDa homohexamer. EB-NSAP shares a conserved sequence motif not only with several lipid phosphatases and the mammalian glucose-6-phosphatases, but also with the vanadium-containing chloroperoxidase (CPO) of Curvularia inaequalis. Comparison of the crystal structures of EB-NSAP and CPO reveals striking similarity in the active site structures. In addition, the topology of the EB-NSAP core shows considerable similarity to the fold of the active site containing part of the monomeric 67 kDa CPO, despite the lack of further sequence identity. These two enzymes are apparently related by divergent evolution. We have also determined the crystal structure of EB-NSAP complexed with the transition-state analog molybdate. Structural comparison of the native enzyme and the enzyme-molybdate complex reveals that the side-chain of His150, a putative catalytic residue, moves toward the molybdate so that it forms a hydrogen bond with the metal oxyanion when the molybdenum forms a covalent bond with NE2 of His189. (+info)Prochiral selectivity in H(2)O(2)-promoted oxidation of arylalkanols catalysed by chloroperoxidase. The role of the interactions between the OH group and the amino-acid residues in the enzyme active site. (6/107)
The H(2)O(2)-promoted oxidations of (R)-[alpha-(2)H(1)]-and (S)-[alpha-(2)H(1)]-arylalkanols catalysed by chloroperoxidase (CPO) from Caldariomyces fumago have been investigated. It has been found that with (R)-[alpha-(2)H(1)]-alcohols, the oxidation involves almost exclusively the cleavage of the C-H bond, whereas in the case of the oxidation of (S)-[alpha-(2)H(1)]-alcohols, the C-D bond is preferentially broken. These results clearly indicate that the reactions of corresponding undeuterated arylalkanols are characterized by a high prochiral selectivity, involving the cleavage of the pro-S C-H bond. This prochiral selectivity is poorly influenced by the electronic effect of ring substituents, whereas it decreases with the length of the carbon lateral chain, in the order: benzyl alcohol > 2-phenylethanol > 3-phenylpropanol. Molecular binding studies showed that the main factor directing the docking of the substrate in such a specific orientation in the enzyme active site is the interaction between the alcoholic OH group and the residue Glu183. This interaction is likely to drive both the stereochemistry and the regiochemistry of these reactions. A bifurcated hydrogen bond involving the OH group, the carboxylate oxygen of Glu183 and the oxoferryl oxygen might also be operating. (+info)Expression of the Caldariomyces fumago chloroperoxidase in Aspergillus niger and characterization of the recombinant enzyme. (7/107)
The Caldariomyces fumago chloroperoxidase was successfully expressed in Aspergillus niger. The recombinant enzyme was produced in the culture medium as an active protein and could be purified by a three-step purification procedure. The catalytic behavior of recombinant chloroperoxidase (rCPO) was studied and compared with that of native CPO. The specific chlorination activity (47 units/nmol) of rCPO and its pH optimum (pH 2.75) were very similar to those of native CPO. rCPO catalyzes the oxidation of various substrates in comparable yields and selectivities to native CPO. Indole was oxidized to 2-oxindole with 99% selectivity and thioanisole to the corresponding R-sulfoxide (enantiomeric excess >98%). Incorporation of (18)O from labeled H(2)18O(2) into the oxidized products was 100% in both cases. (+info)Roles of water in heme peroxidase and catalase mechanisms. (8/107)
A water molecule is coproduced with the Compound I intermediate in the reactions of native heme peroxidases and catalases with hydrogen peroxide. As a result of water release/rebinding from/to the coproduct formation site the Compound I intermediate may exist in two forms: a "wet" form, Compound I(H(2)O), in which a water molecule is present at or near the site of coproduct water formation, and Compound I, in which the coproduct water formation site is "dry." It is postulated that the absence or presence of a water molecule at this site provides the structural basis for a redox pathway switching mechanism, such that the transition states for 2-electron equivalent reduction of Compound I intermediates are accessible in the dry form, but that in the wet form only 1-electron equivalent processes are possible, unless release of water can be stimulated. This concept provides the basis of a general mechanism in which the classical functional distinction between catalases and peroxidases, as well as the more complex behavior observed in halide oxidation and halogenation reactions, appear as particular cases in which variations in the degree of retention of water at the coproduct formation site influence Compound I reactivity. (+info)Chloride peroxidase is an enzyme that contains heme as a cofactor and is responsible for catalyzing the oxidation of chloride ions (Cl-) to hypochlorous acid (HOCl) using hydrogen peroxide (H2O2) as a substrate. This reaction plays a crucial role in the microbial defense system of certain organisms, such as the halophilic archaea. The enzyme is also known as chloroperoxidase or CPO.
The chemical reaction catalyzed by chloride peroxidase can be represented as follows:
Cl- + H2O2 → HOCl + H2O
Hypochlorous acid is a powerful oxidizing agent that can kill or inhibit the growth of various microorganisms, making it an important component of the immune system in some organisms. Chloride peroxidase has attracted significant interest from researchers due to its potential applications in biotechnology and environmental protection, such as in the development of new disinfection methods and the removal of pollutants from water.
Peroxidases are a group of enzymes that catalyze the oxidation of various substrates using hydrogen peroxide (H2O2) as the electron acceptor. These enzymes contain a heme prosthetic group, which plays a crucial role in their catalytic activity. Peroxidases are widely distributed in nature and can be found in plants, animals, and microorganisms. They play important roles in various biological processes, including defense against oxidative stress, lignin degradation, and host-pathogen interactions. Some common examples of peroxidases include glutathione peroxidase, which helps protect cells from oxidative damage, and horseradish peroxidase, which is often used in laboratory research.
Chlorides are simple inorganic ions consisting of a single chlorine atom bonded to a single charged hydrogen ion (H+). Chloride is the most abundant anion (negatively charged ion) in the extracellular fluid in the human body. The normal range for chloride concentration in the blood is typically between 96-106 milliequivalents per liter (mEq/L).
Chlorides play a crucial role in maintaining electrical neutrality, acid-base balance, and osmotic pressure in the body. They are also essential for various physiological processes such as nerve impulse transmission, maintenance of membrane potentials, and digestion (as hydrochloric acid in the stomach).
Chloride levels can be affected by several factors, including diet, hydration status, kidney function, and certain medical conditions. Increased or decreased chloride levels can indicate various disorders, such as dehydration, kidney disease, Addison's disease, or diabetes insipidus. Therefore, monitoring chloride levels is essential for assessing a person's overall health and diagnosing potential medical issues.
Horseradish peroxidase (HRP) is not a medical term, but a type of enzyme that is derived from the horseradish plant. In biological terms, HRP is defined as a heme-containing enzyme isolated from the roots of the horseradish plant (Armoracia rusticana). It is widely used in molecular biology and diagnostic applications due to its ability to catalyze various oxidative reactions, particularly in immunological techniques such as Western blotting and ELISA.
HRP catalyzes the conversion of hydrogen peroxide into water and oxygen, while simultaneously converting a variety of substrates into colored or fluorescent products that can be easily detected. This enzymatic activity makes HRP a valuable tool in detecting and quantifying specific biomolecules, such as proteins and nucleic acids, in biological samples.
Glutathione peroxidase (GPx) is a family of enzymes with peroxidase activity whose main function is to protect the organism from oxidative damage. They catalyze the reduction of hydrogen peroxide, lipid peroxides, and organic hydroperoxides to water or corresponding alcohols, using glutathione (GSH) as a reducing agent, which is converted to its oxidized form (GSSG). There are several isoforms of GPx found in different tissues, including GPx1 (also known as cellular GPx), GPx2 (gastrointestinal GPx), GPx3 (plasma GPx), GPx4 (also known as phospholipid hydroperoxide GPx), and GPx5-GPx8. These enzymes play crucial roles in various biological processes, such as antioxidant defense, cell signaling, and apoptosis regulation.
Peroxidase is a type of enzyme that catalyzes the chemical reaction in which hydrogen peroxide (H2O2) is broken down into water (H2O) and oxygen (O2). This enzymatic reaction also involves the oxidation of various organic and inorganic compounds, which can serve as electron donors.
Peroxidases are widely distributed in nature and can be found in various organisms, including bacteria, fungi, plants, and animals. They play important roles in various biological processes, such as defense against oxidative stress, breakdown of toxic substances, and participation in metabolic pathways.
The peroxidase-catalyzed reaction can be represented by the following chemical equation:
H2O2 + 2e- + 2H+ → 2H2O
In this reaction, hydrogen peroxide is reduced to water, and the electron donor is oxidized. The peroxidase enzyme facilitates the transfer of electrons between the substrate (hydrogen peroxide) and the electron donor, making the reaction more efficient and specific.
Peroxidases have various applications in medicine, industry, and research. For example, they can be used for diagnostic purposes, as biosensors, and in the treatment of wastewater and medical wastes. Additionally, peroxidases are involved in several pathological conditions, such as inflammation, cancer, and neurodegenerative diseases, making them potential targets for therapeutic interventions.
Cytochrome-c peroxidase is an enzyme found in the inner membrane of mitochondria, which are the energy-producing structures in cells. It plays a crucial role in the electron transport chain, a series of complexes that generate energy in the form of ATP through a process called oxidative phosphorylation.
The enzyme's primary function is to catalyze the conversion of hydrogen peroxide (H2O2) into water (H2O) and oxygen (O2). This reaction helps protect the cell from the harmful effects of hydrogen peroxide, which can damage proteins, lipids, and DNA if left unchecked.
Cytochrome-c peroxidase contains a heme group, which is a prosthetic group consisting of an iron atom surrounded by a porphyrin ring. This heme group is responsible for the enzyme's ability to undergo redox reactions, where it cycles between its oxidized and reduced states during the catalytic cycle.
The medical relevance of cytochrome-c peroxidase lies in its role in cellular metabolism and energy production. Dysfunctions in the electron transport chain or oxidative phosphorylation processes, including those involving cytochrome-c peroxidase, can lead to various mitochondrial disorders and diseases, such as neurodegenerative conditions, muscle weakness, and metabolic abnormalities. However, it is essential to note that the study of this enzyme and its role in health and disease is still an active area of research.
Chloride channels are membrane proteins that form hydrophilic pores or gaps, allowing the selective passage of chloride ions (Cl-) across the lipid bilayer of cell membranes. They play crucial roles in various physiological processes, including regulation of neuronal excitability, maintenance of resting membrane potential, fluid and electrolyte transport, and pH and volume regulation of cells.
Chloride channels can be categorized into several groups based on their structure, function, and mechanism of activation. Some of the major classes include:
1. Voltage-gated chloride channels (ClC): These channels are activated by changes in membrane potential and have a variety of functions, such as regulating neuronal excitability and transepithelial transport.
2. Ligand-gated chloride channels: These channels are activated by the binding of specific ligands or messenger molecules, like GABA (gamma-aminobutyric acid) or glycine, and are involved in neurotransmission and neuromodulation.
3. Cystic fibrosis transmembrane conductance regulator (CFTR): This is a chloride channel primarily located in the apical membrane of epithelial cells, responsible for secreting chloride ions and water to maintain proper hydration and mucociliary clearance in various organs, including the lungs and pancreas.
4. Calcium-activated chloride channels (CaCCs): These channels are activated by increased intracellular calcium concentrations and participate in various physiological processes, such as smooth muscle contraction, neurotransmitter release, and cell volume regulation.
5. Swelling-activated chloride channels (ClSwells): Also known as volume-regulated anion channels (VRACs), these channels are activated by cell swelling or osmotic stress and help regulate cell volume and ionic homeostasis.
Dysfunction of chloride channels has been implicated in various human diseases, such as cystic fibrosis, myotonia congenita, epilepsy, and certain forms of cancer.
Ascorbate peroxidases (AHPX) are a group of enzymes that use ascorbic acid (vitamin C) as a reducing cofactor to catalyze the conversion of hydrogen peroxide (H2O2) into water (H2O) and oxygen (O2). This reaction helps protect cells from oxidative damage caused by the accumulation of H2O2, a byproduct of various metabolic processes. Ascorbate peroxidases are primarily found in plants, algae, and cyanobacteria, where they play a crucial role in the detoxification of reactive oxygen species generated during photosynthesis.
Eosinophil peroxidase (EPO) is an enzyme that is primarily found in the granules of eosinophils, which are a type of white blood cell that plays a role in the immune response. EPO is involved in the destruction of certain types of parasites and also contributes to the inflammatory response in allergic reactions and other diseases.
EPO catalyzes the conversion of hydrogen peroxide to hypochlorous acid, which is a potent oxidizing agent that can kill or inhibit the growth of microorganisms. EPO also plays a role in the production of other reactive oxygen species, which can contribute to tissue damage and inflammation in certain conditions.
Elevated levels of EPO in tissues or bodily fluids may be indicative of eosinophil activation and degranulation, which can occur in various diseases such as asthma, allergies, parasitic infections, and some types of cancer. Measuring EPO levels can be useful in the diagnosis and monitoring of these conditions.
Iodide peroxidase, also known as iodide:hydrogen peroxide oxidoreductase, is an enzyme that belongs to the family of oxidoreductases. Specifically, it is a peroxidase that uses iodide as its physiological reducing substrate. This enzyme catalyzes the oxidation of iodide by hydrogen peroxide to produce iodine, which plays a crucial role in thyroid hormone biosynthesis.
The systematic name for this enzyme is iodide:hydrogen-peroxide oxidoreductase (iodinating). It is most commonly found in the thyroid gland, where it helps to produce and regulate thyroid hormones by facilitating the iodination of tyrosine residues on thyroglobulin, a protein produced by the thyroid gland.
Iodide peroxidase requires a heme cofactor for its enzymatic activity, which is responsible for the oxidation-reduction reactions it catalyzes. The enzyme's ability to iodinate tyrosine residues on thyroglobulin is essential for the production of triiodothyronine (T3) and thyroxine (T4), two critical hormones that regulate metabolism, growth, and development in mammals.
Vinyl Chloride is not a medical term, but rather a chemical compound. It's an organochloride with the formula C2H3Cl, and it's a colorless gas at room temperature that is used primarily in the production of polyvinyl chloride (PVC) plastics.
However, Vinyl Chloride is relevant to medical professionals because exposure to this compound has been linked to an increased risk of a rare form of liver cancer called hepatic angiosarcoma, as well as other health problems such as neurological damage and immune system suppression. Therefore, occupational exposure to Vinyl Chloride is regulated by organizations like the Occupational Safety and Health Administration (OSHA) in the United States.
Sodium Chloride is defined as the inorganic compound with the chemical formula NaCl, representing a 1:1 ratio of sodium and chloride ions. It is commonly known as table salt or halite, and it is used extensively in food seasoning and preservation due to its ability to enhance flavor and inhibit bacterial growth. In medicine, sodium chloride is used as a balanced electrolyte solution for rehydration and as a topical wound irrigant and antiseptic. It is also an essential component of the human body's fluid balance and nerve impulse transmission.
I'm sorry for any confusion, but "Polyvinyl Chloride" (PVC) is not a medical term. It is a type of synthetic plastic polymer material. PVC is commonly used in various industrial, commercial, and consumer products, such as pipes, cable insulation, clothing, and inflatable items.
If you have any medical concerns or questions, please provide them, and I would be happy to help you find a relevant answer.
Hydrogen peroxide (H2O2) is a colorless, odorless, clear liquid with a slightly sweet taste, although drinking it is harmful and can cause poisoning. It is a weak oxidizing agent and is used as an antiseptic and a bleaching agent. In diluted form, it is used to disinfect wounds and kill bacteria and viruses on the skin; in higher concentrations, it can be used to bleach hair or remove stains from clothing. It is also used as a propellant in rocketry and in certain industrial processes. Chemically, hydrogen peroxide is composed of two hydrogen atoms and two oxygen atoms, and it is structurally similar to water (H2O), with an extra oxygen atom. This gives it its oxidizing properties, as the additional oxygen can be released and used to react with other substances.
Guaiacol is not a medical term per se, but it is a chemical compound with potential applications in the medical field. Here's a general definition:
Guaiacol (also known as 2-methoxyphenol) is an organic compound that belongs to the class of phenols. It is a colorless or slightly yellow oily liquid with a characteristic smoky odor, and it is soluble in alcohol and ether but only sparingly soluble in water. Guaiacol occurs naturally in the smoke of wood fires and is also found in certain plants, such as guaiacum and creosote bush. It has antimicrobial properties and is used in some medical and industrial applications, including as a precursor for the synthesis of other chemicals.
Catalase is a type of enzyme that is found in many living organisms, including humans. Its primary function is to catalyze the decomposition of hydrogen peroxide (H2O2) into water (H2O) and oxygen (O2). This reaction helps protect cells from the harmful effects of hydrogen peroxide, which can be toxic at high concentrations.
The chemical reaction catalyzed by catalase can be represented as follows:
H2O2 + Catalase → H2O + O2 + Catalase
Catalase is a powerful antioxidant enzyme that plays an important role in protecting cells from oxidative damage. It is found in high concentrations in tissues that produce or are exposed to hydrogen peroxide, such as the liver, kidneys, and erythrocytes (red blood cells).
Deficiency in catalase activity has been linked to several diseases, including cancer, neurodegenerative disorders, and aging. On the other hand, overexpression of catalase has been shown to have potential therapeutic benefits in various disease models, such as reducing inflammation and oxidative stress.
Mercuric chloride, also known as corrosive sublimate, is defined medically as a white or colorless crystalline compound used historically as a topical antiseptic and caustic. It has been used in the treatment of various skin conditions such as warts, thrush, and some parasitic infestations. However, its use is limited nowadays due to its high toxicity and potential for serious side effects, including kidney damage, digestive problems, and nervous system disorders. It is classified as a hazardous substance and should be handled with care.
Selenium is a trace element that is essential for the proper functioning of the human body. According to the medical definitions provided by the National Institutes of Health (NIH), selenium is a component of several major metabolic pathways, including thyroid hormone metabolism, antioxidant defense systems, and immune function.
Selenium is found in a variety of foods, including nuts (particularly Brazil nuts), cereals, fish, and meat. It exists in several forms, with selenomethionine being the most common form found in food. Other forms include selenocysteine, which is incorporated into proteins, and selenite and selenate, which are inorganic forms of selenium.
The recommended dietary allowance (RDA) for selenium is 55 micrograms per day for adults. While selenium deficiency is rare, chronic selenium deficiency can lead to conditions such as Keshan disease, a type of cardiomyopathy, and Kaschin-Beck disease, which affects the bones and joints.
It's important to note that while selenium is essential for health, excessive intake can be harmful. High levels of selenium can cause symptoms such as nausea, vomiting, hair loss, and neurological damage. The tolerable upper intake level (UL) for selenium is 400 micrograms per day for adults.
Lactoperoxidase is a type of peroxidase enzyme that is present in various secretory fluids, including milk, saliva, and tears. In milk, lactoperoxidase plays an important role in the natural defense system by helping to protect against microbial growth. It does this by catalyzing the oxidation of thiocyanate ions (SCN-) in the presence of hydrogen peroxide (H2O2) to produce hypothiocyanite (OSCN-), which is a potent antimicrobial agent.
Lactoperoxidase is a glycoprotein with a molecular weight of approximately 78 kDa, and it is composed of four identical subunits, each containing a heme group that binds to the hydrogen peroxide molecule during the enzymatic reaction. Lactoperoxidase has been studied for its potential therapeutic applications in various fields, including oral health, food preservation, and wound healing.
Chloride peroxidase
Haloperoxidase
Bromide
Peroxidase
Bromide peroxidase
List of MeSH codes (D08)
CPO
Bromine
Organobromine chemistry
Eosinophil peroxidase
Aryl halide
Hypobromite
Myeloperoxidase
Bis(trifluoromethyl)peroxide
ELISpot
Thyroid
Chlorite dismutase
Organoselenium chemistry
List of EC numbers (EC 1)
Heme
Lanthanum
Jeewanu
Glucose
3,3'-Diaminobenzidine
Blue bottle experiment
Hypochlorite
Ebselen
Iodide
Arsenic biochemistry
Human nutrition
Chloride peroxidase - Wikipedia
Search result - BRENDA Enzyme Database
CBRNE - Vomiting Agents - Dm, Da, Dc: Practice Essentials, Background, Pathophysiology
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DeCS
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Steven Robert Blanke - Research & Scholarship
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MMTB
Gene locus Report for: oenob-q04f06
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Horseradish2
- The catalytic acid base, required to cleave the peroxide O-O bond, is glutamic acid rather than histidine as in horseradish peroxidase. (wikipedia.org)
- Labeled with horseradish peroxidase (HRP). (biotrend.com)
Manganese3
- we ivestigated how microbial fuel cell (MFC) performance can be affected by laccase and manganese peroxidase (MnP) enzymes as catalysts in the cathode compartment. (liu.se)
- Decolorization of synthetic dyes by a new manganese peroxidase-producing white rot fungus. (liu.se)
- 2015). Ligninolytic enzyme systems consist mainly of manganese peroxidase, lignin peroxidase (LiP), and laccase. (ncsu.edu)
Lignin1
- Lignin peroxidase (LiP), which has been studied extensively in white-rot Basidiomycetes with regard to bio-pulping and bio-bleaching, plays a role in the biodegradation of plant cell wall lignin. (ncsu.edu)
Catalase4
- The heme-containing chloroperoxidase (CPO) exhibits peroxidase, catalase and cytochrome P450-like activities in addition to catalyzing halogenation reactions. (wikipedia.org)
- The activities of antioxidative enzymes such as superoxide dismutase, catalase, ascorbate peroxidase, guaiacol peroxidase and glutathione reductase tended to increase after salt (90~150mM sodium chloride) treatments. (ncu.edu.tw)
- Gene expression of four oxidative stress markers as well as catalase and peroxidase activities and content of glutathione, total carbonyl, polyphenolics and chlorophyll were quantified. (cardiff.ac.uk)
- Results showed that in saline conditions, XGOs dramatically increased catalase gene expression and enzymatic activity, peroxidase activity, and chlorophyll a/b ratio, while reducing protein oxidation and total polyphenols. (cardiff.ac.uk)
Enzyme glutathione peroxidase2
- The oxido-reductase enzyme glutathione peroxidase 4 (GPX4) governs Salmonella Typhimurium-induced neutrophil transepithelial migration. (umassmed.edu)
- Selenium (Se) is a part of the enzyme glutathione peroxidase, which metabolizes hydroperoxides formed from polyunsaturated fatty acids. (msdmanuals.com)
Bromide1
- In the presence of the enzymes, the fluorescence bleaching was dependent of chloride (Cl−) and bromide (Br−), which makes the assay able to distinguish the halogenating from the peroxidase activity. (unesp.br)
Glutathione reductase1
- After a 20 to 44 hour incubation period in less than 0.05 millimoles of the chlorides of Cd(2+), Zn(2+) and Hg(2+), there was no increase of malonaldehyde (542789) or in the activity of glutathione peroxidase and glutathione reductase. (cdc.gov)
Hydrogen peroxide3
- This enzyme combines the inorganic substrates chloride and hydrogen peroxide to produce the equivalent of Cl+, which replaces a proton in hydrocarbon substrate: R-H + Cl− + H2O2 + H+ → R-Cl + 2 H2O In fact the source of "Cl+" is hypochlorous acid (HOCl). (wikipedia.org)
- The systematic name of this enzyme class is chloride:hydrogen-peroxide oxidoreductase. (wikipedia.org)
- Is the protein surrounding the active site critical for hydrogen peroxide reduction by selenoprotein glutathione peroxidase? (umassmed.edu)
Eosinophil1
- Myeloperoxidase (MPO) and eosinophil peroxidase (EPO) are enzymes present in neutrophil and eosinophil leukocytes, respectively. (unesp.br)
Assay2
- Assay by immunoelectrophoresis resulted in a single precipitin arc against anti-Peroxidase, anti-Donkey IgG, anti-Donkey IgG F(ab')2 and anti-Donkey Serum. (rockland.com)
- In conclusion, this assay can differentiate the peroxidase and halogenating activity of MPO and EPO. (unesp.br)
0.151
- Supplied as a liquid in 0.01M phosphate, 0.15M sodium chloride, pH 7.3. (biotrend.com)
Cytochrome1
- Herein, we demonstrate that cytochrome c (Cyt c ) showed peroxidase activity on IGA as a component of complexes III and IV. (biologists.com)
Antibody3
- Donkey IgG F(ab')2 fragment Peroxidase conjugated secondary antibody reagents are ideal for ELISA, western blotting, Immunohistochemistry, Fluorescence Microscopy, Flow Cytometry as well as other antibody detection methods. (rockland.com)
- Biotinylated anti-human IgG labeled with strepavidin-peroxidase is used to detect the patient's antibody. (cdc.gov)
- More than 50% of these patients have high serum antithyroid peroxidase antibody levels, and nearly 50% have overt hypothyroidism. (medscape.com)
Oxidoreductases1
- This enzyme belongs to the family of oxidoreductases, specifically those acting on a peroxide as acceptors (peroxidases). (wikipedia.org)
Serum3
- Donkey IgG F(ab')2 fragment Peroxidase conjugated - Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. (rockland.com)
- HUMAN ALBUMIN Peroxidase conjugated was prepared from normal serum by a multi-step process including selective precipitation and tandem chromatography followed by extensive dialysis against the buffer stated above. (rockland.com)
- The antigen is prepared from a modified Venereal Disease Research Laboratory (VDRL) antigen suspension containing choline chloride to eliminate the need to heat-inactivate serum, ethylene-diamine-tetra-acetic acid (EDTA) to enhance the stability of the suspension, and finely divided charcoal particles as a visualizing agent. (cdc.gov)
Protein1
- Ammonium chloride-ammonium hydroxide Buffer Solution is a high quality research product used as buffer for protein crystallization. (moleculardepot.com)
Descriptor1
- Glutathione Peroxidase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (umassmed.edu)
Characterization1
- 2: Zheng L, Lian L, Nie J, Song Y, Yan S, Yin D, Song W. Development of an ammonium chloride-enhanced thermal-assisted-ESI LC-HRMS method for the characterization of chlorinated paraffins. (moleculardepot.com)
Activity4
- 2,3,7,8-Tetrachlorodibenzo- p -dioxin as an antiestrogen: Effect on rat uterine peroxidase activity. (cdc.gov)
- The signals of IGA based on peroxidase activity were obtained using enhanced chemiluminescence solution. (biologists.com)
- Diagnosis of selenium deficiency is made clinically or sometimes by measuring glutathione peroxidase activity or plasma selenium , but neither of these tests is readily available. (msdmanuals.com)
- Saliva contains a number of components, including various electrolytes, glycoproteins, enzymes, and mucus, as well as secretory immunoglobulin A, lactoferrin, lysozyme, and peroxidase-with the latter 4 components important in that they exhibit antibacterial activity. (medscape.com)
Calcium2
- α-Amylase is heterogeneous enzyme which requires calcium and chloride ions for its action. (thejcdp.com)
- Four cations: Sodium, potassium, calcium, and magnesium Two accompanying anions: Chloride and phosphorus Daily requirements range from. (msdmanuals.com)
Behavior2
- 5: Sass MD. Effect of ammonium chloride on osmotic behavior of red cells in nonelectrolytes. (moleculardepot.com)
- Effects of ammonium chloride on urinary pH and cigarette smoking behavior. (moleculardepot.com)
Organic2
- Chloride peroxidase (EC 1.11.1.10) is a family of enzymes that catalyzes the chlorination of organic compounds. (wikipedia.org)
- An enzyme that catalyzes the chlorination of a range of organic molecules, forming stable carbon-chloride bonds. (bvsalud.org)
Total1
- This graph shows the total number of publications written about "Glutathione Peroxidase" by people in this website by year, and whether "Glutathione Peroxidase" was a major or minor topic of these publications. (umassmed.edu)
Important1
- Antioxidants in the saliva are chiefly composed of uric acid, CAT, peroxidase, and some other important enzymes. (thejcdp.com)
Salt3
- Receptor model source attributions for Utah's Salt Lake City airshed and the impacts of wintertime secondary ammonium nitrate and ammonium chloride aerosol. (moleculardepot.com)
- Lipid peroxidation tended to decrease with lower concentrations of salt (30~90mM sodium chloride) treatments, but tended to increase with higher concentrations of salt (120~150mM sodium chloride) treatments. (ncu.edu.tw)
- A. thaliana plants were grown in liquid media and after 15 days they were treated by a salt shock with 100 mM of sodium chloride, with or without XGOs at 0.1 mg L-1. (cardiff.ac.uk)
