Mixed Function Oxygenases
Cytochrome P-450 Enzyme System
Heme Oxygenase (Decyclizing)
Aryl Hydrocarbon Hydroxylases
Nonheme Iron Proteins
Molecular Sequence Data
Amino Acid Sequence
Decreased liver and lung drug-metabolizing activity in mice treated with Corynebacterium parvum. (1/3676)Injections of killed suspensions of Corynebacterium parvum (i.p.) in young male mice were followed by time- and dose-dependent decreases in the drug-metabolizing activity of liver microsomes and lung homogenates. In vitro assays with model substrates [aminopyrine, aniline, p-nitroanisole, and benzo(a)pyrene] were used to quantitate drug-metabolizing activity. It is likely that such decreases in mixed function oxidases activity will act to significantly alter the pharmacokinetics of concurrently or subsequently administered drugs. The results provide a possible mechanism to explain several previously reported immunochemotherapeutic interactions. (+info)
Patterns of evolutionary rate variation among genes of the anthocyanin biosynthetic pathway. (2/3676)The anthocyanin biosynthetic pathway is responsible for the production of anthocyanin pigments in plant tissues and shares a number of enzymes with other biochemical pathways. The six core structural genes of this pathway have been cloned and characterized in two taxonomically diverse plant species (maize and snapdragon). We have recently cloned these genes for a third species, the common morning glory, Ipomoea purpurea. This additional information provides an opportunity to examine patterns of evolution among genes within a single biochemical pathway. We report here that upstream genes in the anthocyanin pathway have evolved substantially more slowly than downstream genes and suggest that this difference in evolutionary rates may be explained by upstream genes being more constrained because they participate in several different biochemical pathways. In addition, regulatory genes associated with the anthocyanin pathway tend to evolve more rapidly than the structural genes they regulate, suggesting that adaptive evolution of flower color may be mediated more by regulatory than by structural genes. Finally, for individual anthocyanin genes, we found an absence of rate heterogeneity among three major angiosperm lineages. This rate constancy contrasts with an accelerated rate of evolution of three CHS-like genes in the Ipomoea lineage, indicating that these three genes have diverged without coordinated adjustment by other pathway genes. (+info)
The PalkBFGHJKL promoter is under carbon catabolite repression control in Pseudomonas oleovorans but not in Escherichia coli alk+ recombinants. (3/3676)The alk genes are located on the OCT plasmid of Pseudomonas oleovorans and encode an inducible pathway for the utilization of n-alkanes as carbon and energy sources. We have investigated the influence of alternative carbon sources on the induction of this pathway in P. oleovorans and Escherichia coli alk+ recombinants. In doing so, we confirmed earlier reports that induction of alkane hydroxylase activity in pseudomonads is subject to carbon catabolite repression. Specifically, synthesis of the monooxygenase component AlkB is repressed at the transcriptional level. The alk genes have been cloned into plasmid pGEc47, which has a copy number of about 5 to 10 per cell in both E. coli and pseudomonads. Pseudomonas putida GPo12 is a P. oleovorans derivative cured of the OCT plasmid. Upon introduction of pGEc47 in this strain, carbon catabolite repression of alkane hydroxylase activity was reduced significantly. In cultures of recombinant E. coli HB101 and W3110 carrying pGEc47, induction of AlkB and transcription of the alkB gene were no longer subject to carbon catabolite repression. This suggests that carbon catabolite repression of alkane degradation is regulated differently in Pseudomonas and in E. coli strains. These results also indicate that PalkBFGHJKL, the Palk promoter, might be useful in attaining high expression levels of heterologous genes in E. coli grown on inexpensive carbon sources which normally trigger carbon catabolite repression of native expression systems in this host. (+info)
Properties of 5-aminolaevulinate synthetase and its relationship to microsomal mixed-function oxidation in the southern armyworm (Spodoptera eridania). (4/3676)1. Activity of 5-aminolaevulinate synthetase was measured in the midgut and other tissues of the last larval instar of the southern armyworm (Spodoptera eridania Cramer, formerly Prodenia eridania Cramer). 2. Optimum conditions for measuring the activity were established with respect to all variables involved and considerable differences from those reported for mammalian enzyme preparations were found. 3. Maximum activity (20 nmol/h per mg of protein) occurs 18-24 h after the fifth moult and thereafter decreases to trace amounts as the larvae age and approach pupation. 4. Synthetase activity was rapidly induced by oral administration (in the diet) of pentamethylbenzene, phenobarbital, diethyl 1,4-dihydro-2,4,6-trimethylpyridine-3, 5-dicarboxylate, and 2-allyl-2-isopropylacetamide. 5. Puromycin inhibited the induction of synthetase by pentamethylbenzene. 6. Induction of 5-aminolaevulinate synthetase correlated well with the induction of microsomal N-demethylation of p-chloro-N-methylaniline, except for phenobarbital, which induced the microsomal oxidase relatively more than the synthetase. (+info)
Null mutation in IRE1 gene inhibits overproduction of microsomal cytochrome P450Alk1 (CYP 52A3) and proliferation of the endoplasmic reticulum in Saccharomyces cerevisiae. (5/3676)Overproduction of microsomal cytochrome P450Alk1 (P450Alk1) of Candida maltosa in Saccharomyces cerevisiae resulted in an extensive proliferation of endoplasmic reticulum (ER) and induction of Kar2p and Pdi1p. The ire1 null mutation severely suppressed ER proliferation, reduced the level of functional P450Alk1, and showed no induction of these ER chaperones, suggesting that the function of Ire1p is required for ER proliferation upon the overproduction of P450Alk1. Cerulenin, a potent inhibitor of lipid biosynthesis, also induced these chaperones in an Ire1p-dependent manner and limited the production of functional P450Alk1. These results imply that Ire1p may function to restore the balance between membrane proteins and lipids of the ER when the ER is relatively overcrowded by membrane proteins. (+info)
Structure of a cytochrome P450-redox partner electron-transfer complex. (6/3676)The crystal structure of the complex between the heme- and FMN-binding domains of bacterial cytochrome P450BM-3, a prototype for the complex between eukaryotic microsomal P450s and P450 reductase, has been determined at 2.03 A resolution. The flavodoxin-like flavin domain is positioned at the proximal face of the heme domain with the FMN 4.0 and 18.4 A from the peptide that precedes the heme-binding loop and the heme iron, respectively. The heme-binding peptide represents the most efficient and coupled through-bond electron pathway to the heme iron. Substantial differences between the FMN-binding domains of P450BM-3 and microsomal P450 reductase, observed around the flavin-binding sites, are responsible for different redox properties of the FMN, which, in turn, control electron flow to the P450. (+info)
Immunophilins, Refsum disease, and lupus nephritis: the peroxisomal enzyme phytanoyl-COA alpha-hydroxylase is a new FKBP-associated protein. (7/3676)FKBP52 (FKBP59, FKBP4) is a "macro" immunophilin that, although sharing high structural and functional homologies in its amino-terminal domain with FKBP12 (FKBP1), does not have immunosuppressant activity when complexed with FK506, unlike FKBP12. To investigate the physiological function of FKBP52, we used the yeast two-hybrid system as an approach to find its potential protein partners and, from that, its cellular role. This methodology, which already has allowed us to find the FK506-binding protein (FKBP)-associated protein FAP48, also led to the detection of another FKBP-associated protein. Determination of the sequence of this protein permitted its identification as phytanoyl-CoA alpha-hydroxylase (PAHX), a peroxisomal enzyme that so far was unknown as an FKBP-associated protein. Inactivation of this enzyme is responsible for Refsum disease in humans. The protein also corresponds to the mouse protein LN1, which could be involved in the progress of lupus nephritis. We show here that PAHX has the physical capacity to interact with the FKBP12-like domain of FKBP52, but not with FKBP12, suggesting that it is a particular and specific target of FKBP52. Whereas the binding of calcineurin to FKBP12 is potentiated by FK506, the specific association of PAHX and FKBP52 is maintained in the presence of FK506. This observation suggests that PAHX is a serious candidate for studying the cellular signaling pathway(s) involving FKBP52 in the presence of immunosuppressant drugs. (+info)
Involvement of cytochromes P-450 2E1 and 3A4 in the 5-hydroxylation of salicylate in humans. (8/3676)Hydroxylation of salicylate into 2,3 and 2,5-dihydroxybenzoic acids (2,3-DHBA and 2,5-DHBA) by human liver microsomal preparations was investigated. Kinetic studies demonstrated that salicylate was 5-hydroxylated with two apparent Km: one high-affinity Km of 606 microM and one low-affinity Km greater than 2 mM. Liver microsomes prepared from 15 human samples catalyzed the formation of 2,5-DHBA at metabolic rate of 21.7 +/- 8.5 pmol/mg/min. The formation of 2, 3-DHBA was not P-450 dependent. Formation of 2,5-DHBA was inhibited by 36 +/- 14% following preincubation of microsomes with diethyldithiocarbamate, a mechanism-based selective inhibitor of P-450 2E1. Furthermore, the efficiency of inhibition was significantly correlated with four catalytic activities specific to P-450 2E1, whereas the residual activity was correlated with three P-450 3A4 catalytic activities. Troleandomycin, a mechanism-based inhibitor selective to P-450 3A4, inhibited by 30 +/- 12% the 5-hydroxylation of salicylate, and this inhibition was significantly correlated with nifedipine oxidation, specific to P-450 3A4. The capability of seven recombinant human P-450s to hydroxylate salicylate demonstrated that P-450 2E1 and 3A4 contributed to 2, 5-DHBA formation in approximately equal proportions. The Km values of recombinant P-450 2E1 and 3A4, 280 and 513 microM, respectively, are in the same range as the high-affinity Km measured with human liver microsomes. The plasmatic metabolic ratio 2,5-DHBA/salicylate, measured 2 h after ingestion of 1 g acetylsalicylate, was increased 3-fold in 12 alcoholic patients at the beginning of their withdrawal period versus 15 control subjects. These results confirm that P-450 2E1, inducible by ethanol, is involved in the 5-hydroxylation of salicylate in humans. Furthermore, this ratio was still increased by 2-fold 1 week after ethanol withdrawal. This finding suggests that P-450 3A4, known to be also inducible by alcoholic beverages, plays an important role in this increase, because P-450 2E1 returned to normal levels in less than 3 days after ethanol withdrawal. Finally, in vivo and in vitro data demonstrated that P-450 2E1 and P-450 3A4, both inducible by alcohols, catalyzed the 5-hydroxylation of salicylate. (+info)
Mixed-function oxygenases are a class of enzymes that catalyze the oxidation of a wide range of substrates, including drugs, toxins, and endogenous compounds. These enzymes typically contain a non-heme iron or copper atom in their active site, which is coordinated by a variety of amino acid residues. Mixed-function oxygenases are involved in a variety of biological processes, including drug metabolism, xenobiotic detoxification, and the synthesis of important biological molecules such as cholesterol and bile acids. They are also involved in the metabolism of many environmental pollutants, including polycyclic aromatic hydrocarbons and halogenated hydrocarbons. In the medical field, mixed-function oxygenases are important because they play a key role in the metabolism of many drugs, which can affect their efficacy and toxicity. For example, the cytochrome P450 family of mixed-function oxygenases is responsible for the metabolism of many commonly prescribed drugs, including anti-inflammatory drugs, antidepressants, and anticoagulants. Understanding the role of these enzymes in drug metabolism is important for optimizing drug therapy and minimizing adverse drug reactions.
In the medical field, oxygenases are enzymes that catalyze the addition of oxygen to a substrate molecule. These enzymes are involved in a wide range of biological processes, including the metabolism of drugs, the synthesis of hormones and other signaling molecules, and the detoxification of harmful substances. There are many different types of oxygenases, each with its own specific substrate and reaction mechanism. Some examples of oxygenases include cytochrome P450 enzymes, which are involved in the metabolism of drugs and other xenobiotics, and peroxidases, which are involved in the detoxification of reactive oxygen species. Oxygenases play a critical role in maintaining the health of living organisms, and their dysfunction can lead to a variety of diseases and disorders. For example, mutations in certain cytochrome P450 enzymes can lead to drug metabolism disorders, while deficiencies in peroxidases can contribute to the development of oxidative stress-related diseases.
Piperonyl Butoxide (PBO) is an insect repellent and insecticide that is commonly used in combination with other active ingredients, such as permethrin or DEET, to provide longer-lasting protection against insect bites and the transmission of insect-borne diseases. It works by disrupting the nervous system of insects, making it difficult for them to move, feed, and reproduce. In the medical field, PBO is used as a preventative measure against insect-borne diseases such as malaria, dengue fever, and Zika virus. It is often applied to clothing, bed nets, and other surfaces to repel mosquitoes and other insects that can transmit these diseases. PBO is also used in veterinary medicine to protect animals from insect bites and the spread of insect-borne diseases. It is important to note that PBO can be harmful if ingested or applied to the skin in large amounts. It is also not recommended for use on infants or young children, pregnant women, or people with certain medical conditions. As with any insect repellent or insecticide, it is important to follow the instructions on the label and to use PBO in a safe and responsible manner.
Aminopyrine N-demethylase (APND) is an enzyme that is involved in the metabolism of aminopyrine, a drug that is used to test for liver function. The enzyme is primarily found in the liver and is responsible for converting aminopyrine into its active metabolite, which can then be eliminated from the body. APND activity is often used as a measure of liver function, as it is influenced by factors such as liver damage or disease. Low levels of APND activity may indicate liver dysfunction or damage, while high levels may indicate liver disease or other conditions that affect liver function.
7-Alkoxycoumarin O-dealkylase is an enzyme that is involved in the metabolism of certain drugs and chemicals in the body. It is responsible for breaking down a specific type of molecule called 7-alkoxycoumarins, which are found in some medications and natural compounds. The enzyme catalyzes the removal of an alkyl group (a carbon-based molecule) from the 7-position of the coumarin molecule, resulting in the formation of a new compound. This process is an important step in the elimination of these substances from the body, and any disruption in the activity of the enzyme can affect the metabolism and elimination of the drug or chemical.
Benzopyrene Hydroxylase (CYP1A1) is an enzyme that plays a crucial role in the metabolism of polycyclic aromatic hydrocarbons (PAHs), including the potent carcinogen benzo[a]pyrene. It is encoded by the CYP1A1 gene and is primarily expressed in the liver, lungs, and skin. The primary function of CYP1A1 is to catalyze the hydroxylation of PAHs, which converts them into more polar and water-soluble metabolites that can be more easily excreted from the body. This process is an important step in the body's defense against the toxic and carcinogenic effects of PAHs. Deficiency or mutations in the CYP1A1 gene can lead to reduced activity of the enzyme, which can result in increased susceptibility to PAH-induced toxicity and cancer. In addition, exposure to certain environmental factors, such as cigarette smoke and air pollution, can induce the expression of CYP1A1, leading to increased metabolism of PAHs and potentially increased cancer risk.
Antipyrine is a medication that is used to reduce fever and relieve pain. It is a member of a class of drugs called antipyretics, which are used to lower body temperature. Antipyrine is available over-the-counter and is often used to treat mild to moderate fever and pain associated with conditions such as the flu, colds, and headaches. It is also sometimes used to treat muscle pain and stiffness. Antipyrine works by blocking the production of prostaglandins, which are chemicals that are involved in the body's response to injury and infection and can cause fever and pain.
Phenobarbital is a barbiturate medication that is primarily used to treat seizures, particularly in people with epilepsy. It is also used to treat anxiety, insomnia, and other conditions that cause restlessness or agitation. Phenobarbital works by increasing the activity of gamma-aminobutyric acid (GABA), a neurotransmitter that helps to calm the brain and reduce seizures. It is available in both oral and injectable forms and is typically taken several times a day. Phenobarbital can cause side effects such as drowsiness, dizziness, and nausea, and it may interact with other medications. It is important to take phenobarbital exactly as prescribed by a healthcare provider to avoid the risk of side effects or overdose.
Oxidoreductases are a class of enzymes that catalyze redox reactions, which involve the transfer of electrons from one molecule to another. These enzymes play a crucial role in many biological processes, including metabolism, energy production, and detoxification. In the medical field, oxidoreductases are often studied in relation to various diseases and conditions. For example, some oxidoreductases are involved in the metabolism of drugs and toxins, and changes in their activity can affect the efficacy and toxicity of these substances. Other oxidoreductases are involved in the production of reactive oxygen species (ROS), which can cause cellular damage and contribute to the development of diseases such as cancer and aging. Oxidoreductases are also important in the diagnosis and treatment of certain diseases. For example, some oxidoreductases are used as markers of liver disease, and changes in their activity can indicate the severity of the disease. In addition, some oxidoreductases are targets for drugs used to treat diseases such as cancer and diabetes. Overall, oxidoreductases are a diverse and important class of enzymes that play a central role in many biological processes and are the subject of ongoing research in the medical field.
Allylisopropylacetamide (also known as acetamide allyl isopropyl ether or 2-(allyloxy)acetamide) is a chemical compound that has been used in the medical field as an anticonvulsant and anesthetic. It is a white, crystalline solid that is soluble in water and organic solvents. In the past, allylisopropylacetamide was used to treat seizures and other neurological disorders, but its use has been largely discontinued due to concerns about its toxicity and potential for adverse side effects. It is not currently approved for use in humans by any regulatory agency. In the laboratory, allylisopropylacetamide is used as a solvent and as a starting material for the synthesis of other compounds. It has also been studied for its potential as a fungicide and as a corrosion inhibitor.
Skatole is a chemical compound that is produced by the breakdown of tryptophan in the human body. It is also known as 3-methylindole or 3-methyl-1H-indole. Skatole is a foul-smelling compound that is often associated with the smell of feces. It is produced by the gut bacteria of some animals, including humans, and is present in small amounts in the urine and feces of these animals. In the medical field, skatole is sometimes used as a diagnostic tool to identify certain types of gastrointestinal disorders, such as inflammatory bowel disease or colon cancer. It is also used as a marker of exposure to certain drugs, such as the anti-inflammatory drug indomethacin.
The cytochrome P-450 enzyme system is a group of enzymes that are responsible for the metabolism of a wide variety of drugs, toxins, and other substances in the body. These enzymes are found in the liver, lungs, and other organs, and they play a critical role in the detoxification of harmful substances and the elimination of drugs from the body. The cytochrome P-450 enzymes are classified into several families, each of which is responsible for the metabolism of specific types of compounds. For example, the CYP3A family is responsible for the metabolism of a wide variety of drugs, including many commonly prescribed medications. The CYP2D6 family is responsible for the metabolism of some antidepressants, antipsychotics, and other drugs. The activity of the cytochrome P-450 enzyme system can be affected by a variety of factors, including genetic variations, age, sex, and the presence of other medications. In some cases, these factors can lead to differences in the metabolism of drugs, which can affect their effectiveness and the risk of side effects. Overall, the cytochrome P-450 enzyme system plays a critical role in the metabolism of drugs and other substances in the body, and understanding its function is important for the safe and effective use of medications.
Biotransformation is a process in the body where foreign substances, such as drugs, toxins, and environmental chemicals, are converted into more water-soluble and easily excreted forms. This process occurs in the liver and involves various enzymes that modify the chemical structure of the substance, making it less toxic and more easily eliminated from the body. Biotransformation can occur through two main pathways: phase I and phase II. In phase I, enzymes called cytochrome P450 oxidize the substance, adding or removing hydrogen atoms, which can make the substance more reactive and potentially toxic. In phase II, enzymes such as glutathione S-transferases and UDP-glucuronosyltransferases add functional groups to the substance, making it more water-soluble and easier to excrete. Biotransformation is an important process in the body as it helps to detoxify harmful substances and prevent them from building up in the body. However, certain factors such as genetics, age, liver function, and certain medications can affect the rate and efficiency of biotransformation, which can impact the effectiveness and safety of drugs and other substances in the body.
Ketoglutaric acid is a chemical compound that is involved in the metabolism of amino acids in the body. It is a key intermediate in the citric acid cycle, also known as the Krebs cycle or the tricarboxylic acid cycle, which is a series of chemical reactions that generate energy in the form of ATP (adenosine triphosphate) from glucose and other nutrients. In the medical field, ketoglutaric acid is sometimes used as a dietary supplement or as a treatment for certain medical conditions. For example, it has been suggested that ketoglutaric acid may have potential as a treatment for cancer, as it has been shown to have anti-tumor effects in some studies. It has also been suggested that ketoglutaric acid may have potential as a treatment for other conditions, such as Alzheimer's disease and Parkinson's disease, although more research is needed to confirm these potential benefits. It is important to note that the use of ketoglutaric acid as a dietary supplement or as a treatment for medical conditions is not well-established, and more research is needed to fully understand its potential benefits and risks. It is always a good idea to talk to a healthcare professional before starting any new supplement or treatment.
Dioxygenases are a class of enzymes that catalyze the addition of molecular oxygen (O2) to a substrate molecule. These enzymes are involved in a wide range of biological processes, including the metabolism of lipids, carbohydrates, and amino acids, as well as the detoxification of harmful substances. Dioxygenases can be classified into several different types based on the specific chemical reaction they catalyze and the type of substrate they act on. For example, cytochrome P450 enzymes are a type of dioxygenase that are involved in the metabolism of drugs and other xenobiotics, while lipoxygenases are involved in the metabolism of fatty acids. Dioxygenases play an important role in maintaining the health of living organisms, but they can also contribute to the development of disease. For example, certain mutations in dioxygenase genes can lead to the production of abnormal enzymes that are unable to function properly, which can result in a variety of health problems. Additionally, some dioxygenases can produce reactive oxygen species (ROS) as a byproduct of their activity, which can cause damage to cellular components and contribute to the development of diseases such as cancer and aging.
Biliverdine is a bile pigment that is produced when the liver breaks down hemoglobin, the protein in red blood cells that carries oxygen. It is a greenish-yellow compound that is excreted in the bile and can be detected in the urine and stool of individuals with liver disease or other conditions that affect bilirubin metabolism. In the medical field, biliverdine is often used as a diagnostic tool to help identify liver disease or other conditions that affect bilirubin metabolism. It can also be used as a treatment for certain types of liver disease, such as hepatitis C, by helping to reduce the amount of bilirubin in the blood and prevent liver damage.
Aryl Hydrocarbon Hydroxylases (AHHs) are a group of enzymes that are involved in the metabolism of aromatic hydrocarbons, such as polycyclic aromatic hydrocarbons (PAHs) and halogenated aromatic hydrocarbons (HAHs). These enzymes are primarily found in the liver and are responsible for the oxidation of these compounds to their corresponding hydroxylated derivatives. AHHs play an important role in the detoxification of these compounds, as the hydroxylated derivatives are more water-soluble and can be more easily excreted from the body. In addition, the hydroxylation of aromatic hydrocarbons can also lead to the formation of reactive intermediates, such as quinones, which can be further metabolized or detoxified by other enzymes. AHHs are also involved in the metabolism of other compounds, such as certain drugs and hormones. Mutations in the genes encoding AHHs can lead to impaired metabolism of these compounds, which can result in toxicity or other health effects. In the medical field, AHHs are often studied in the context of their role in the metabolism of environmental pollutants and their potential health effects. For example, exposure to PAHs and HAHs has been linked to an increased risk of cancer and other health problems, and AHHs are thought to play a key role in this process.
Nonheme iron proteins are a class of proteins that contain iron but do not have the heme prosthetic group. Heme is a complex organic molecule that contains an iron atom coordinated to a porphyrin ring, and it is found in many proteins involved in oxygen transport, such as hemoglobin and myoglobin. Nonheme iron proteins, on the other hand, contain iron that is not coordinated to a porphyrin ring and is instead bound to other ligands, such as histidine or cysteine residues. Nonheme iron proteins play a variety of roles in biological systems. For example, they are involved in the metabolism of iron, the detoxification of reactive oxygen species, and the catalysis of various chemical reactions. Some examples of nonheme iron proteins include ferritin, transferrin, and cytochrome P450 enzymes.
NADP stands for Nicotinamide Adenine Dinucleotide Phosphate. It is a coenzyme that plays a crucial role in various metabolic processes in the body, including the metabolism of carbohydrates, fats, and proteins. NADP is involved in the conversion of glucose to glycogen, the breakdown of fatty acids, and the synthesis of amino acids. It is also involved in the process of photosynthesis in plants, where it acts as a carrier of electrons. In the medical field, NADP is often used as a supplement to support various metabolic processes and to enhance energy production in the body.
Heme is a complex organic molecule that contains iron and is a vital component of hemoglobin, myoglobin, and other proteins involved in oxygen transport and storage in living organisms. It is also a component of various enzymes involved in metabolism and detoxification processes. In the medical field, heme is often used as a diagnostic tool to detect and monitor certain medical conditions, such as anemia (a deficiency of red blood cells or hemoglobin), liver disease (which can affect heme synthesis), and certain types of cancer (which can produce abnormal heme molecules). Heme is also used in the production of certain medications, such as heme-based oxygen carriers for use in patients with sickle cell disease or other conditions that affect oxygen transport. Additionally, heme is a component of some dietary supplements and is sometimes used to treat certain types of anemia.
Corynebacterium diphtheriae is a gram-positive, aerobic, non-motile bacterium that is the causative agent of diphtheria, a highly contagious and potentially life-threatening infectious disease. The bacterium produces a potent toxin that can cause damage to the respiratory tract, skin, and other tissues, leading to symptoms such as fever, sore throat, difficulty breathing, and swelling of the neck. In severe cases, diphtheria can lead to heart failure, paralysis, and death. Treatment typically involves antibiotics to kill the bacteria and antitoxin to neutralize the toxin. Vaccination is also available to prevent diphtheria.
Beta-carotene 15,15'-monooxygenase (BCMO) is an enzyme that plays a crucial role in the metabolism of beta-carotene, a provitamin A carotenoid found in many fruits and vegetables. In the human body, beta-carotene is converted into vitamin A, which is essential for maintaining healthy vision, skin, and immune function. BCMO is responsible for converting beta-carotene into two different forms of vitamin A: retinal and retinoic acid. BCMO is primarily found in the liver and small intestine, where it is involved in the absorption and metabolism of dietary beta-carotene. It is also expressed in other tissues, including the retina, where it plays a critical role in the conversion of beta-carotene into vitamin A for vision. Mutations in the BCMO gene can lead to a deficiency in the enzyme, resulting in a condition called beta-carotene deficiency. This condition can cause a range of symptoms, including night blindness, dry skin, and impaired immune function.
In the medical field, "iron" refers to a mineral that is essential for the production of red blood cells, which carry oxygen throughout the body. Iron is also important for the proper functioning of the immune system, metabolism, and energy production. Iron deficiency is a common condition that can lead to anemia, a condition in which the body does not have enough red blood cells to carry oxygen to the body's tissues. Symptoms of iron deficiency anemia may include fatigue, weakness, shortness of breath, and pale skin. Iron supplements are often prescribed to treat iron deficiency anemia, and dietary changes may also be recommended to increase iron intake. However, it is important to note that excessive iron intake can also be harmful, so it is important to follow the recommended dosage and consult with a healthcare provider before taking any iron supplements.
Oxidoreductases, O-demethylating are a group of enzymes that catalyze the removal of a methyl group from a substrate molecule. These enzymes are important in the metabolism of many drugs and other compounds, as well as in the detoxification of harmful substances. They are classified as oxidoreductases because they involve the transfer of electrons from one molecule to another. The O in the name refers to the fact that the methyl group is being removed from an oxygen-containing molecule. These enzymes play a crucial role in maintaining the balance of chemicals in the body and are involved in many physiological processes.
Carbon monoxide (CO) is a colorless, odorless, and tasteless gas that is produced when fossil fuels such as coal, oil, and gas are burned incompletely. In the medical field, carbon monoxide poisoning is a serious condition that occurs when a person inhales high levels of the gas, which can interfere with the body's ability to transport oxygen to the tissues. Carbon monoxide binds to hemoglobin in red blood cells, forming carboxyhemoglobin, which reduces the amount of oxygen that can be carried by the blood. This can lead to symptoms such as headache, dizziness, nausea, confusion, and shortness of breath. In severe cases, carbon monoxide poisoning can cause unconsciousness, seizures, and even death. The medical treatment for carbon monoxide poisoning involves removing the person from the source of the gas and providing oxygen therapy to help restore normal oxygen levels in the blood. In some cases, additional medical treatment may be necessary to manage symptoms and prevent complications.
Catechols are a class of organic compounds that contain a catechol group, which is a hydroxybenzene group with two hydroxyl (-OH) groups attached to a benzene ring. Catechols are found naturally in many plants and animals, and they are also synthesized in the body as part of various metabolic processes. In the medical field, catechols are often used as antioxidants and anti-inflammatory agents. They have been shown to have a number of potential health benefits, including reducing the risk of heart disease, improving blood flow, and protecting against oxidative stress. Catechols are also used in the production of a variety of pharmaceuticals and medical devices, including drugs for treating high blood pressure, heart disease, and Parkinson's disease. They are also used in the manufacturing of dyes, pigments, and other industrial chemicals.
Biodegradation, Environmental in the medical field refers to the process by which microorganisms break down and consume organic matter in the environment. This process is important in the management of medical waste, as it helps to reduce the amount of waste that is sent to landfills and reduces the risk of environmental contamination. Biodegradation can occur naturally, through the action of microorganisms in the environment, or it can be accelerated through the use of biodegradable materials or biodegradation agents. In the medical field, biodegradation is often used to dispose of medical waste, such as bandages, gauze, and other materials that are contaminated with bodily fluids or other potentially infectious materials.
Procollagen-Proline Dioxygenase (PPOD) is an enzyme that plays a crucial role in the process of collagen synthesis. Collagen is a protein that is found in the extracellular matrix of connective tissues, such as skin, bones, and tendons. PPOD is responsible for the conversion of proline, an amino acid found in collagen, to hydroxyproline, a modified form of proline that is essential for the stability and strength of collagen fibers. PPOD is a copper-containing enzyme that is found in the endoplasmic reticulum of cells. It catalyzes the oxidation of proline to hydroxyproline in the presence of molecular oxygen and a copper-containing cofactor. The hydroxylation of proline is a critical step in the formation of stable collagen fibers, as hydroxyproline is a key component of the triple helix structure of collagen. In the medical field, PPOD is of interest because it plays a role in the development of several diseases, including osteoporosis, fibrosis, and cancer. For example, mutations in the PPOD gene have been associated with a rare genetic disorder called prolyl 3-hydroxylase deficiency, which is characterized by abnormal collagen synthesis and bone fragility. Additionally, PPOD has been shown to be upregulated in several types of cancer, and its inhibition has been proposed as a potential therapeutic strategy for treating these diseases.
Heme Oxygenase-1 (HO-1) is an enzyme that plays a crucial role in the metabolism of heme, a component of hemoglobin found in red blood cells. HO-1 is induced in response to various stressors, including inflammation, oxidative stress, and exposure to toxins. The primary function of HO-1 is to break down heme into biliverdin, carbon monoxide (CO), and iron (Fe). Biliverdin is then converted into bilirubin, which is excreted from the body. CO has several biological effects, including vasodilation and anti-inflammatory properties. Fe is recycled and used for the synthesis of new heme. HO-1 has been shown to have a number of beneficial effects in the body, including protection against oxidative stress, inflammation, and tissue damage. It has been implicated in the prevention and treatment of a variety of diseases, including cardiovascular disease, neurodegenerative disorders, and cancer. In the medical field, HO-1 is often studied as a potential therapeutic target for the treatment of various diseases. For example, drugs that induce HO-1 activity have been shown to have anti-inflammatory and anti-cancer effects in preclinical studies. However, more research is needed to fully understand the role of HO-1 in disease and to develop effective therapies that target this enzyme.
In the medical field, benzoates are a class of organic compounds that are commonly used as preservatives in a variety of pharmaceutical and personal care products. They are derivatives of benzoic acid, which is a naturally occurring compound found in many fruits and vegetables. Benzoates are used in medical products to prevent the growth of bacteria, mold, and yeast, which can cause spoilage and other problems. They are also used as a preservative in some topical medications, such as creams and ointments, to help prevent the growth of bacteria and other microorganisms that can cause infections. Some common examples of benzoates used in medical products include sodium benzoate, potassium benzoate, and ethyl benzoate. These compounds are generally considered safe for use in medical products, but in some cases, they may cause allergic reactions or other adverse effects in some people. It is important for healthcare providers to carefully consider the potential risks and benefits of using benzoates in medical products, and to monitor patients for any signs of adverse reactions.
In the medical field, catalysis refers to the acceleration of a chemical reaction by a catalyst. A catalyst is a substance that increases the rate of a chemical reaction without being consumed or altered in the process. Catalysts are commonly used in medical research and drug development to speed up the synthesis of compounds or to optimize the efficiency of chemical reactions. For example, enzymes are biological catalysts that play a crucial role in many metabolic processes in the body. In medical research, enzymes are often used as catalysts to speed up the synthesis of drugs or to optimize the efficiency of chemical reactions involved in drug metabolism. Catalysis is also used in medical imaging techniques, such as magnetic resonance imaging (MRI), where contrast agents are used to enhance the visibility of certain tissues or organs. These contrast agents are often synthesized using catalytic reactions to increase their efficiency and effectiveness. Overall, catalysis plays a critical role in many areas of medical research and drug development, helping to accelerate the synthesis of compounds and optimize the efficiency of chemical reactions.
In the medical field, oxygen is a gas that is essential for the survival of most living organisms. It is used to treat a variety of medical conditions, including respiratory disorders, heart disease, and anemia. Oxygen is typically administered through a mask, nasal cannula, or oxygen tank, and is used to increase the amount of oxygen in the bloodstream. This can help to improve oxygenation of the body's tissues and organs, which is important for maintaining normal bodily functions. In medical settings, oxygen is often used to treat patients who are experiencing difficulty breathing due to conditions such as pneumonia, chronic obstructive pulmonary disease (COPD), or asthma. It may also be used to treat patients who have suffered from a heart attack or stroke, as well as those who are recovering from surgery or other medical procedures. Overall, oxygen is a critical component of modern medical treatment, and is used in a wide range of clinical settings to help patients recover from illness and maintain their health.
Crystallography, X-ray is a technique used in the medical field to study the structure of biological molecules, such as proteins and nucleic acids, by analyzing the diffraction patterns produced by X-rays passing through the sample. This technique is used to determine the three-dimensional structure of these molecules, which is important for understanding their function and for developing new drugs and therapies. X-ray crystallography is a powerful tool that has been instrumental in advancing our understanding of many important biological processes and diseases.
Bacterial proteins are proteins that are synthesized by bacteria. They are essential for the survival and function of bacteria, and play a variety of roles in bacterial metabolism, growth, and pathogenicity. Bacterial proteins can be classified into several categories based on their function, including structural proteins, metabolic enzymes, regulatory proteins, and toxins. Structural proteins provide support and shape to the bacterial cell, while metabolic enzymes are involved in the breakdown of nutrients and the synthesis of new molecules. Regulatory proteins control the expression of other genes, and toxins can cause damage to host cells and tissues. Bacterial proteins are of interest in the medical field because they can be used as targets for the development of antibiotics and other antimicrobial agents. They can also be used as diagnostic markers for bacterial infections, and as vaccines to prevent bacterial diseases. Additionally, some bacterial proteins have been shown to have therapeutic potential, such as enzymes that can break down harmful substances in the body or proteins that can stimulate the immune system.
Hemin is a naturally occurring iron-containing porphyrin compound that is found in red blood cells. It is the primary component of hemoglobin, the protein responsible for carrying oxygen from the lungs to the body's tissues and carbon dioxide from the tissues back to the lungs. In the medical field, hemin is used as a medication to treat a rare genetic disorder called porphyria, which is characterized by the accumulation of toxic byproducts of heme metabolism in the body. Hemin is also used in the treatment of certain types of anemia, such as acute intermittent porphyria, and as a supplement to increase iron levels in people with iron deficiency anemia. Hemin has also been studied for its potential therapeutic effects in other conditions, such as cancer, neurodegenerative diseases, and infectious diseases. However, more research is needed to fully understand its potential uses and side effects.
In the medical field, an amino acid sequence refers to the linear order of amino acids in a protein molecule. Proteins are made up of chains of amino acids, and the specific sequence of these amino acids determines the protein's structure and function. The amino acid sequence is determined by the genetic code, which is a set of rules that specifies how the sequence of nucleotides in DNA is translated into the sequence of amino acids in a protein. Each amino acid is represented by a three-letter code, and the sequence of these codes is the amino acid sequence of the protein. The amino acid sequence is important because it determines the protein's three-dimensional structure, which in turn determines its function. Small changes in the amino acid sequence can have significant effects on the protein's structure and function, and this can lead to diseases or disorders. For example, mutations in the amino acid sequence of a protein involved in blood clotting can lead to bleeding disorders.
List of MeSH codes (D08)
Cytochrome P450 reductase
Bacterial cell structure
Bradykinin receptor B2
Iron in biology
Effect of conjugated equine estrogens on oxidative metabolism in middle-aged and elderly postmenopausal women
Bioluminescence - Wikipedia
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Enantiomeric metabolic interactions and stereoselective human methadone metabolism.
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Hypoxia, hypoxia-inducible factors (HIF), HIF hydroxylases and oxygen sensing. - Oxford Cardiovascular Science
- Hepatic microsomal cytochrome-P-450 mixed function oxygenase system catalyzes conversion of methylene - chloride to carbon-monoxide and chloride and a second metabolic pathway yields formaldehyde (50000) and inorganic halide. (cdc.gov)
- Although cytochrome P-450 dependent mixed function oxygenases are important in the activation of arylamines, there are target tissues for arylamines which do not contain these oxygenases. (mun.ca)
- To confirm this hypothesis, sediment and interstitial water samples from Black Duck Cove were assessed with a comprehensive set of biotests and chemical assays.Residual oil in the sediments had limited effect on hepatic CYP1A protein levels and mixed function oxygenase (MFO) induction in winter flounder (Pleuronectes americanus). (canada.ca)
- Heme oxygenase-1 (Hmox1) catalyzes the conversion of heme to biliverdin, carbon monoxide (CO), and ferrous iron (Fe 2+ ). (springer.com)
- METHODOLOGY/PRINCIPAL FINDINGS: We previously detected Bone morphogenetic protein 7 (Bmp7) expression in the urorectal mesenchyme (URM), and have shown that loss of Bmp7 function results in the arrest of cloacal septation. (bvsalud.org)
- Heme oxygenase-1 (Hmox1) is a stress-inducible protein crucial in heme catabolism. (springer.com)
- Subsequently, multiple HIF isoforms have been shown to have overlapping but non-redundant functions, controlling expression of genes involved in diverse processes such as angiogenesis, vascular tone, metal transport, glycolysis, mitochondrial function, cell growth and survival. (ox.ac.uk)
- Myocyte-restricted Hmox1 transgenic mice exposed to MI exhibited significantly improved survival and LV function, lower interstitial fibrosis and oxidative stress. (springer.com)
- Moreover, AA metabolites produced in different locations by cyclo-oxygenase can have opposing effects. (medscape.com)
- Nonsteroidal inflammatory drugs with a mode of action that inhibits cyclo-oxygenase have mixed effects on CVD risk. (medscape.com)
- As a class, cyclo-oxygenase inhibitory NSAIDs may be associated with gastrointestinal, renal and hepatic toxicity. (nih.gov)
- Oxygenase and peroxygenase enzymes generate intermediates at their active sites which bring about the controlled functionalization of inert C-H bonds in substrates, such as in the enzymatic conversion of methane to methanol. (ebsco.com)
- Hepatic microsomal cytochrome-P-450 mixed function oxygenase system catalyzes conversion of methylene-chloride to carbon-monoxide and chloride and a second metabolic pathway yields formaldehyde (50000) and inorganic halide. (cdc.gov)
- RANITIDINE does not inhibit the hepatic cytochrome P450 linked mixed function oxygenase enzyme system. (cathaydrug.com)
- Mul-treated mice had an attenuated cardiac injured response and improved cardiac function after DOX injection. (hindawi.com)
- The following HIV (human immunodeficiency virus) , we looked into the function of the enzyme using mammalian mobile or portable knockdowns in the mixed transcriptomics and also metabolomics investigation. (micrornalibrary.com)
- NSAIDs may inhibit the prostaglandins that maintain normal homeostatic function. (nih.gov)
- Transient and reversible changes in liver function tests can occur. (cathaydrug.com)
- Goji berries have been extensively researched for their ability to generate general feelings of well-being, improve neurologic/psychological traits, support better gastrointestinal health and bowel functions, help build stronger musculoskeletal systems, and improve cardiovascular health. (oliveoildivine.com)
- Despite implementing waste management programs, occasionally small volumes of NDWW could be mixed with DWW and be released to the sewage system. (scirp.org)
- to be present when characteristic pathological abnormalities in the lung result in deterioration of normal lung function, and ARDS to be a specific form of lung injury with diverse causes, characterized pathologically by diffuse alveolar damage and a breakdown in both the barrier and gas exchange functions of the lung, resulting in proteinaceous alveolar edema and hypoxem ia. (org.pk)