An allylic compound that acts as a suicide inactivator of CYTOCHROME P450 by covalently binding to its heme moiety or surrounding protein.
Derivatives of acetamide that are used as solvents, as mild irritants, and in organic synthesis.
An enzyme of the transferase class that catalyzes condensation of the succinyl group from succinyl coenzyme A with glycine to form delta-aminolevulinate. It is a pyridoxyal phosphate protein and the reaction occurs in mitochondria as the first step of the heme biosynthetic pathway. The enzyme is a key regulatory enzyme in heme biosynthesis. In liver feedback is inhibited by heme. EC 2.3.1.37.
A barbituric acid derivative that acts as a nonselective central nervous system depressant. It potentiates GAMMA-AMINOBUTYRIC ACID action on GABA-A RECEPTORS, and modulates chloride currents through receptor channels. It also inhibits glutamate induced depolarizations.
1,4-Dihydro-2,4,6-trimethyl-3,5-pyridinedicarboxylic acid diethyl ester.
A drug-metabolizing enzyme of the hepatic microsomal oxidase system which catalyzes the oxidation of the N-methyl group of ethylmorphine with the formation of formaldehyde.
A group of compounds containing the porphin structure, four pyrrole rings connected by methine bridges in a cyclic configuration to which a variety of side chains are attached. The nature of the side chain is indicated by a prefix, as uroporphyrin, hematoporphyrin, etc. The porphyrins, in combination with iron, form the heme component in biologically significant compounds such as hemoglobin and myoglobin.
**Maleates** are organic compounds that contain a carboxylic acid group and a hydroxyl group attached to adjacent carbon atoms, often used as intermediates in the synthesis of pharmaceuticals and other chemicals, or as drugs themselves, such as maleic acid or its salts.
The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.
Chloro(7,12-diethenyl-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-dipropanoato(4-)-N(21),N(22),N(23),N(24)) ferrate(2-) dihydrogen.
A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism.
An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis.
Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.

delta-Aminolevulinate synthetases in the liver cytosol fraction and mitochondria of mice treated with allylisopropylacetamide and 3,5-dicarbethoxyl-1,4-dihydrocollidine. (1/64)

Hepatic delta-aminolevulinate (ALA) synthetase was induced in mice by the administration of allylisopropylacetamide (AIA) and 3,5-dicarbethoxy-1,4-dihydrocollidine (DDC). In both cases, a significant amount of ALA synthetase accumulated in the liver cytosol fraction as well as in the mitochondria. The apparent molecular weight of the cytosol ALA synthetase was estimated to be 320,000 by gel filtration, but when the cytosol ALA synthetase was subjected to sucrose density gradient centrifugation, it showed a molecular weight of 110,000. In the mitochondria, there were two different sizes of ALA synthetase with molecular weights of 150,000 and 110,000, respectively; the larger enzyme was predominant in DDC-treated mice, whereas in AIA-treated mice and normal mice the enzyme existed mostly in the smaller form. When hemin was injected into mice pretreated with DDC, the molecular size of the mitochondrial ALA synthetase changed from 150,000 to 110,000. The half-life of ALA synthetase in the liver cytosol fraction was about 30 min in both the AIA-treated and DDC-treated mice. The half-life of the mitochondrial ALA synthetase in AIA-treated mice and normal mice was about 60 min, but in DDC-treated mice the half-life was as long as 150 min. The data suggest that the cytosol ALA synthetase of mouse liver is a protein complex with properties very similar to those of the cytosol ALA synthetase of rat liver, which has been shown to be composed of the enzyme active protein and two catalytically inactive binding proteins, and that ALA synthetase may be transferred from the liver cytosol fraction to the mitochondria with a size of about 150,000 daltons, followed by its conversion to enzyme with a molecular weight of 110,000 within the mitochondria. The process of intramitochondrial enzyme degradation seems to be affected in DDC-treated animals.  (+info)

Cytochrome CYP sources of N-alkylprotoporphyrin IX after administration of porphyrinogenic xenobiotics to rats. (2/64)

Cytochrome P-450 (CYP) 3A2 and CYP2C11 are sources of 70 and 30%, respectively, of N-vinylprotoporphyrin IX (N-vinylPP) formation after administration of 3-[(arylthio)ethyl]sydnone (TTMS) to rats. Female rats receiving TTMS were pretreated with dexamethasone, which induces CYP3A1 preferentially to CYP3A2. The resulting 12-fold increase in N-vinylPP formation showed that CYP3A1 was also a source of N-vinylPP. Phenobarbital (PB) pretreatment, which induces CYP2B1/2 and 3A1/2 in male rats, increased N-vinylPP formation after TTMS administration. Troleandomycin, a selective CYP3A inhibitor, was unable to decrease TTMS-mediated N-vinylPP formation in PB-treated male rats, indicating that CYP2B1/2 were sources of N-vinylPP. This conclusion was supported by demonstrating a 15-fold increase in TTMSinduced N-vinylPP formation in female rats after CYP2B1/2 induction with PB pretreatment. Allylispropylacetamide (AIA) inactivates rat CYP2B1/2, 2C6, 2C7, 2C11, and 3A1/2. Troleandomycin was unable to decrease N-AIA protoporphyrin IX adduct (N-AIAPP) formation, showing that CYP3A1/2 were not susceptible to AIA-mediated N-alkylation. N-AIAPP formation in females was approximately 30% of that in males, and thus we attribute 30% of N-AIAPP formation in males to the non-gender-specific isozymes (CYP2C6, 2C7, and/or 2B1/2), whereas approximately 70% originates from CYP2C11. PB treatment in female rats resulted in a 5-fold increase in N-AIAPP formation, showing that CYP2B1/2 were also susceptible to N-alkylation mediated by AIA. 1-Aminobenzotriazole elicited formation of equivalent amounts of N'N-aryl bridged protoporphyrin IX in male and female rat liver, demonstrating that nonselective mechanism-based inactivation is accompanied by nonselective conversion of the CYP heme moieties to N'N-aryl bridged protoporphyrin IX.  (+info)

On the sequence of reactions leading to cytochrome P-450 synthesis-effect of drugs. (3/64)

The effect of phenobarbital on the rates of the synthesis of the protein and heme moieties of cytochromeP-450 has been studied. For this purpose, cytochrome P-450 has been partially purified as its P-420 derivative and the labeled amino acid incorporation into the protein has been studied after subjecting a partially purified preparation to sodium dodecyl sulfate gel electrophoresis. The incorporation studies into the protein species after sodium dodecyl sulfate gel electrophoresis reveal that the drug primarily accelerates the rate of apoptotein synthesis followed by an increase in the rate of heme synthesis. The messenger for apocytochrome P-450 appears to be fairly stable.  (+info)

Cobalt stimulation of heme degradation in the liver. Dissociation of microsomal oxidation of heme from cytochrome P-450. (4/64)

The administration of cobalt to rats caused a marked increase in the oxidative degradation of heme (hematin, iron protoporphyrin-IX) BY HEPATIC MICROSOMAL ENZYMES. The onset of this enzyme stimulation was very rapid, beginning within 2 hours after injection of the metal and reaching its maximum in 16 to 24 hours. During the rapid phase of stimulation, i.e. the first 2 to 4 hours, when heme oxidation was 450% above control values, there was a significant decrease in microsomal oxidative N-demethylation activity and in microsomal oxidative Ndemethylation activity and in microsomal content of heme with an insignificant decrease in cytochrome P-450 content. Within 24 hours the oxidative activity of the microsomal electron transport chain for drugs was decreased to about 30% of the control. However, during the same period the oxidation of heme approached levels 800% above control. During this period there was a further decrease in the microsomal content of heme with a significant decrease in cytochrome P-450 content and an increase in the activity of delta-aminolevulinate synthetase. The activity of delta-aminolevulinate synthetase reached its maximum within 8 hours after cobalt treatment. Repeated injections (at 24-hour intervals) of cobalt were necessary to maintain these changes in microsomal enzyme activities since, after single injections of the metal, these parameters returned to normal within 72 hours. The inducing effect of cobalt on the oxidation of heme could be inhibited by the administration of actinomycin D and puromycin. Furthermore, this stimulatory effect could not be elicited by in vitro treatment of microsomes with cobalt nor could the effect be attributed to any soluble components of the cytoplasm. Cobalt protoporphyrin-IX was less effective than cobalt chloride in stimulating heme oxidation. 3-Amino-1, 2, 4-triazole did not enhance hepatic heme oxidation activity, while allylisopropylacetamide decreased this activity. The oxidative degradation of heme was found not to be cytochrome P-450 dependent since the highly increased levels of heme oxidation in microsomes from cobalt-treated animals could be retained despite the fact that the cytochrome P-450 content of such microsomes was decreased to spectrally undetectable amounts and drug oxidation was eliminated by treatment of the microsomes with 4 M urea. These findings exclude an obligatory role for cytochrome P-450 in the oxidation of heme compounds, although the possibility that this process is a heme-dependent oxidation is not ruled out.  (+info)

Effect of allylisopropylacetamide on Nuclear Ribonucleic Acid synthesis in rat liver. (5/64)

The porphyrogenic drug allylisopropylacetamide, a potent inducer of delta-aminolaevulinate synthetase, specifically increases nucleoplasmic RNA synthesis in rat liver. The drug-mediated increase in nucleoplasmic RNA synthesis is blocked by cycloheximide and haemin, which also inhibit the enzyme induction.  (+info)

Degradation of cytochrome P-450 haem by carbon tetrachloride and 2-allyl-2-isopropylacetamide in rat liver in vivo and in vitro. Involvement of non-carbon monoxide-forming mechanisms. (6/64)

Degradation of intrinsic hepatic [(14)C]haem was analysed as (14)CO formation in living rats and in hepatic microsomal fractions prepared from these animals 16h after pulse-labelling with 5-amino[5-(14)C]laevulinic acid, a precursor that labels bridge carbons of haem in non-erythroid tissues. NADPH-catalysed peroxidation of microsomal lipids in vitro (measured as malondialdehyde) was accompanied by loss of cytochrome P-450 and microsome-associated [(14)C]haem (largely cytochrome P-450 haem), but little (14)CO formation. No additional (14)CO was formed when carbon tetrachloride and 2-allyl-2-isopropylacetamide were added to stimulate lipid peroxidation and increase loss of cytochrome P-450 [(14)C]haem. Because the latter effect persisted despite inhibition of lipid peroxidation with MnCl(2) or phenyl-t-butylnitrone(a spin-trapping agent for free radicals), it was concluded that carbon tetrachloride, as reported for 2-allyl-2-isopropylacetamide, may promote loss of cytochrome P-450 haem through a non-CO-forming mechanism independent of lipid peroxidation. By comparison with breakdown of intrinsic haem, catabolism of [(14)C]methaemalbumin by microsomal haem oxygenase in vitro produced equimolar quantities of (14)CO and bilirubin, although these catabolites reflected only 18% of the degraded [(14)C]haem. This value was increased to 100% by addition of MnCl(2), which suggests that lipid peroxidation may be involved in degradation of exogenous haem to products other than CO. Phenyl-t-butylnitrone completely blocked haem oxygenase activity, which suggests that hydroxy free radicals may represent a species of active oxygen used by this enzyme system. After administration of carbon tetrachloride or 2-allyl-2-isopropylacetamide to labelled rats, hepatic [(14)C]haem was decreased and haem oxygenase activity was unchanged; however, (14)CO excretion was either unchanged (carbon tetrachloride) or decreased (2-allyl-2-isopropylacetamide). These changes were unaffected by cycloheximide pretreatment. From the lack of parallel losses of cytochrome P-450 [(14)C]haem and (14)CO excretion, one may infer that an important fraction of hepatic [(14)C]haem in normal rats is degraded by endogenous pathways not involving CO. We conclude that carbon tetrachloride and 2-allyl-2-isopropylacetamide accelerate catabolism of cytochrome P-450 haem through mechanisms that do not yield CO as an end product, and that are insensitive to cycloheximide and independent of haem oxygenase activity.  (+info)

Characterization of the anticonvulsant profile and enantioselective pharmacokinetics of the chiral valproylamide propylisopropyl acetamide in rodents. (7/64)

1. Propylisopropyl acetamide (PID) is a new chiral amide derivative of valproic acid. The purpose of this study was to evaluate the anticonvulsant activity of PID in rodent models of partial, secondarily generalized and sound-induced generalized seizures which focus on different methods of seizure induction, both acute stimuli, and following short-term plastic changes as a result of kindling, and to assess enantioselectivity and enantiomer-enantiomer interactions in the pharmacokinetics and pharmacodynamics of racemic PID and its pure enantiomers in rodents. 2. Anticonvulsant activity of (S)-PID, (R)-PID and racemic PID was evaluated in the 6 Hz psychomotor seizure model in mice, in the hippocampal kindled rat, and in the Frings audiogenic seizure susceptible mouse. The pharmacokinetics of (S)-PID and (R)-PID was studied in mice and rats. 3. In mice (S)-PID, (R)-PID and racemic PID were effective in preventing the 6 Hz seizures with (R)-PID being significantly (P < 0.05) more potent (ED(50) values 11 mg kg(-1), 46 mg kg(-1) and 57 mg kg(-1) at stimulation intensities of 22, 32 and 44 mA, respectively) than (S)-PID (ED(50) values 20 mg kg(-1), 73 mg kg(-1) and 81 mg kg(-1) at stimulation intensities of 22, 32 and 44 mA, respectively). (S)-PID, (R)-PID and racemic PID also blocked generalized seizures in the Frings mice (ED(50) values 16 mg kg(-1), 20 mg kg(-1) and 19 mg kg(-1) respectively). 4. In the hippocampal kindled rat a dose of 40 mg kg(-1) of (R)- and (S)-PID prevented the secondarily generalized seizure, whereas racemic PID also blocked the expression of partial seizures following an i.p. dose of 40 mg kg(-1). Racemic PID also significantly increased the seizure threshold in this model. 5. Mechanistic studies showed that PID did not affect voltage-sensitive sodium channels or kainate-, GABA- or NMDA- evoked currents. 6. The pharmacokinetics of PID was enantioselective following i.p. administration of individual enantiomers to mice, with (R)-PID having lower clearance and longer half-life than (S)-PID. In rats and mice, no enantioselectivity in the pharmacokinetics of PID was observed following administration of the racemate, which may be due to enantiomer-enantiomer interaction. 7. This study demonstrated that PID has both enantioselective pharmacokinetics and pharmacodynamics. The better anticonvulsant potency of (R)-PID in comparison to (S)-PID may be due to its more favorable pharmacokinetic profile. The enhanced efficacy of the racemate over the individual enantiomers in the kindled rat may be explained by a pharmacokinetic enantiomer-enantiomer interaction in rats. This study also showed the importance of studying the pharmacokinetics and pharmacodynamics of chiral drugs following administration of the individual enantiomers as well as the racemic mixture.  (+info)

Hepatic heme metabolism and its control. (8/64)

This review summarizes heme metabolism and focuses especially upon the control of hepatic heme biosynthesis. Activity of delta-aminolevulinic acid synthetase, the first enzyme of heme biosynthesis, is of primary importance in controlling the overall activity of this biosynthetic pathway. Delta-aminolevulinic acid synthetase is subject to inhibition and repression by heme, and numerous basic and clinical studies support the concept that there exists within hepatocytes a "regulatory" heme pool which controls activity of delta-aminolevulinic acid synthetase. In addition, activity of this enzyme is repressed by feeding, especially by ingestion of carbohydrates (the so-called "glucose effect"). Studies pertaining to the mechanisms underlying this effect are also reviewed. The "glucose effect" appears to be mediated by glucose or perhaps by glucose-6-phosphate or uridine diphosphate glucose, rather than by metabolites further removed from glucose itself. Unlike the situation in E. coli, the "glucose effect" in liver of higher organisms is not mediated by alterations in intracellular concentrations of cyclic AMP. Effects of heavy metals, especially iron, on hepatic heme metabolism are also considered. Iron has been found to inhibit formation and utilization of uroporphyrinogen III and to lead to decreased concentrations of microsomal heme and cytochrome P-450. Administration of large amounts of iron is also associated with an increase in activity of heme oxygenase, a property shared by several other metal ions, most notably cobalt. This effect of iron or cobalt administration is similar to the effect of heme administration in increasing heme oxygenase activity; however, we believe it is unlikely that iron, rather than heme itself, is a physiologic regulator of hepatic heme metabolism, although this hypothesis has lately been proposed.  (+info)

Allylisopropylacetamide is not a term that has a widely accepted or established medical definition. It is a chemical compound with the formula (CH₂CHCH₂)N(C=O)CH(CH₃)₂, and it may have various chemical or industrial uses, but it is not a term that is commonly used in medical contexts.

If you have any specific questions about this compound or its potential uses or effects, I would recommend consulting with a relevant expert, such as a chemist or toxicologist, who can provide more detailed and accurate information based on their expertise and knowledge of the subject.

Acetamides are organic compounds that contain an acetamide functional group, which is a combination of an acetyl group (-COCH3) and an amide functional group (-CONH2). The general structure of an acetamide is R-CO-NH-CH3, where R represents the rest of the molecule.

Acetamides are found in various medications, including some pain relievers, muscle relaxants, and anticonvulsants. They can also be found in certain industrial chemicals and are used as intermediates in the synthesis of other organic compounds.

It is important to note that exposure to high levels of acetamides can be harmful and may cause symptoms such as headache, dizziness, nausea, and vomiting. Chronic exposure has been linked to more serious health effects, including liver and kidney damage. Therefore, handling and use of acetamides should be done with appropriate safety precautions.

5-Aminolevulinate synthase (ALAS) is an enzyme that catalyzes the first step in heme biosynthesis, a metabolic pathway that produces heme, a porphyrin ring with an iron atom at its center. Heme is a crucial component of hemoglobin, cytochromes, and other important molecules in the body.

ALAS exists in two forms: ALAS1 and ALAS2. ALAS1 is expressed in all tissues, while ALAS2 is primarily expressed in erythroid cells (precursors to red blood cells). The reaction catalyzed by ALAS involves the condensation of glycine and succinyl-CoA to form 5-aminolevulinate.

Deficiencies or mutations in the ALAS2 gene can lead to a rare genetic disorder called X-linked sideroblastic anemia, which is characterized by abnormal red blood cell maturation and iron overload in mitochondria.

Phenobarbital is a barbiturate medication that is primarily used for the treatment of seizures and convulsions. It works by suppressing the abnormal electrical activity in the brain that leads to seizures. In addition to its anticonvulsant properties, phenobarbital also has sedative and hypnotic effects, which can be useful for treating anxiety, insomnia, and agitation.

Phenobarbital is available in various forms, including tablets, capsules, and elixirs, and it is typically taken orally. The medication works by binding to specific receptors in the brain called gamma-aminobutyric acid (GABA) receptors, which help to regulate nerve impulses in the brain. By increasing the activity of GABA, phenobarbital can help to reduce excessive neural activity and prevent seizures.

While phenobarbital is an effective medication for treating seizures and other conditions, it can also be habit-forming and carries a risk of dependence and addiction. Long-term use of the medication can lead to tolerance, meaning that higher doses may be needed to achieve the same effects. Abruptly stopping the medication can also lead to withdrawal symptoms, such as anxiety, restlessness, and seizures.

Like all medications, phenobarbital can have side effects, including dizziness, drowsiness, and impaired coordination. It can also interact with other medications, such as certain antidepressants and sedatives, so it is important to inform your healthcare provider of all medications you are taking before starting phenobarbital.

In summary, phenobarbital is a barbiturate medication used primarily for the treatment of seizures and convulsions. It works by binding to GABA receptors in the brain and increasing their activity, which helps to reduce excessive neural activity and prevent seizures. While phenobarbital can be effective, it carries a risk of dependence and addiction and can have side effects and drug interactions.

I apologize, but I am unable to find a medical definition for "dicarbethoxydihydrocollidine." It is possible that this term does not have a specific meaning within the field of medicine. A more general search indicates that dicarbethoxydihydrocollidine may be a chemical compound used in research or industry, but it does not appear to have direct relevance to medical diagnosis, treatment, or health. If you have further questions or need information on a related medical topic, I would be happy to help you with those.

Ethylmorphine-N-demethylase is an enzyme that catalyzes the chemical reaction in the liver responsible for metabolizing (breaking down) the drug ethylmorphine. The enzyme does this by removing a methyl group from the ethylmorphine molecule, converting it into a different compound called normethadone. This enzyme is part of the cytochrome P450 family and is specifically classified as CYP2D6.

The activity of Ethylmorphine-N-demethylase (CYP2D6) can vary widely among individuals, which can affect how they metabolize certain drugs. Some people have multiple copies of the gene that encodes this enzyme and are considered "ultrarapid metabolizers," meaning they break down these drugs very quickly. Others may have reduced or even no activity of this enzyme due to genetic variations, which can lead to slower drug metabolism and potential for adverse effects.

Porphyrins are complex organic compounds that contain four pyrrole rings joined together by methine bridges (=CH-). They play a crucial role in the biochemistry of many organisms, as they form the core structure of various heme proteins and other metalloproteins. Some examples of these proteins include hemoglobin, myoglobin, cytochromes, and catalases, which are involved in essential processes such as oxygen transport, electron transfer, and oxidative metabolism.

In the human body, porphyrins are synthesized through a series of enzymatic reactions known as the heme biosynthesis pathway. Disruptions in this pathway can lead to an accumulation of porphyrins or their precursors, resulting in various medical conditions called porphyrias. These disorders can manifest as neurological symptoms, skin lesions, and gastrointestinal issues, depending on the specific type of porphyria and the site of enzyme deficiency.

It is important to note that while porphyrins are essential for life, their accumulation in excessive amounts or at inappropriate locations can result in pathological conditions. Therefore, understanding the regulation and function of porphyrin metabolism is crucial for diagnosing and managing porphyrias and other related disorders.

"Maleate" is not a medical term in and of itself, but it is a chemical compound that can be found in some medications. Maleic acid or its salts (maleates) are used as a keratolytic agent in topical medications, which means they help to break down and remove dead skin cells. They can also be used as a preservative or a buffering agent in various pharmaceutical preparations.

Maleic acid is a type of organic compound known as a dicarboxylic acid, which contains two carboxyl groups. In the case of maleic acid, these carboxyl groups are located on a single carbon atom, which makes it a cis-conjugated diacid. This structural feature gives maleic acid unique chemical properties that can be useful in various pharmaceutical and industrial applications.

It's worth noting that maleic acid and its salts should not be confused with "maleate" as a gender-specific term, which refers to something related to or characteristic of males.

Heme is not a medical term per se, but it is a term used in the field of medicine and biology. Heme is a prosthetic group found in hemoproteins, which are proteins that contain a heme iron complex. This complex plays a crucial role in various biological processes, including oxygen transport (in hemoglobin), electron transfer (in cytochromes), and chemical catalysis (in peroxidases and catalases).

The heme group consists of an organic component called a porphyrin ring, which binds to a central iron atom. The iron atom can bind or release electrons, making it essential for redox reactions in the body. Heme is also vital for the formation of hemoglobin and myoglobin, proteins responsible for oxygen transport and storage in the blood and muscles, respectively.

In summary, heme is a complex organic-inorganic structure that plays a critical role in several biological processes, particularly in electron transfer and oxygen transport.

Hemin is defined as the iron(III) complex of protoporphyrin IX, which is a porphyrin derivative. It is a naturally occurring substance that is involved in various biological processes, most notably in the form of heme, which is a component of hemoglobin and other hemoproteins. Hemin is also used in medical research and therapy, such as in the treatment of methemoglobinemia and lead poisoning.

The Cytochrome P-450 (CYP450) enzyme system is a group of enzymes found primarily in the liver, but also in other organs such as the intestines, lungs, and skin. These enzymes play a crucial role in the metabolism and biotransformation of various substances, including drugs, environmental toxins, and endogenous compounds like hormones and fatty acids.

The name "Cytochrome P-450" refers to the unique property of these enzymes to bind to carbon monoxide (CO) and form a complex that absorbs light at a wavelength of 450 nm, which can be detected spectrophotometrically.

The CYP450 enzyme system is involved in Phase I metabolism of xenobiotics, where it catalyzes oxidation reactions such as hydroxylation, dealkylation, and epoxidation. These reactions introduce functional groups into the substrate molecule, which can then undergo further modifications by other enzymes during Phase II metabolism.

There are several families and subfamilies of CYP450 enzymes, each with distinct substrate specificities and functions. Some of the most important CYP450 enzymes include:

1. CYP3A4: This is the most abundant CYP450 enzyme in the human liver and is involved in the metabolism of approximately 50% of all drugs. It also metabolizes various endogenous compounds like steroids, bile acids, and vitamin D.
2. CYP2D6: This enzyme is responsible for the metabolism of many psychotropic drugs, including antidepressants, antipsychotics, and beta-blockers. It also metabolizes some endogenous compounds like dopamine and serotonin.
3. CYP2C9: This enzyme plays a significant role in the metabolism of warfarin, phenytoin, and nonsteroidal anti-inflammatory drugs (NSAIDs).
4. CYP2C19: This enzyme is involved in the metabolism of proton pump inhibitors, antidepressants, and clopidogrel.
5. CYP2E1: This enzyme metabolizes various xenobiotics like alcohol, acetaminophen, and carbon tetrachloride, as well as some endogenous compounds like fatty acids and prostaglandins.

Genetic polymorphisms in CYP450 enzymes can significantly affect drug metabolism and response, leading to interindividual variability in drug efficacy and toxicity. Understanding the role of CYP450 enzymes in drug metabolism is crucial for optimizing pharmacotherapy and minimizing adverse effects.

Enzyme induction is a process by which the activity or expression of an enzyme is increased in response to some stimulus, such as a drug, hormone, or other environmental factor. This can occur through several mechanisms, including increasing the transcription of the enzyme's gene, stabilizing the mRNA that encodes the enzyme, or increasing the translation of the mRNA into protein.

In some cases, enzyme induction can be a beneficial process, such as when it helps the body to metabolize and clear drugs more quickly. However, in other cases, enzyme induction can have negative consequences, such as when it leads to the increased metabolism of important endogenous compounds or the activation of harmful procarcinogens.

Enzyme induction is an important concept in pharmacology and toxicology, as it can affect the efficacy and safety of drugs and other xenobiotics. It is also relevant to the study of drug interactions, as the induction of one enzyme by a drug can lead to altered metabolism and effects of another drug that is metabolized by the same enzyme.

Microsomes, liver refers to a subcellular fraction of liver cells (hepatocytes) that are obtained during tissue homogenization and subsequent centrifugation. These microsomal fractions are rich in membranous structures known as the endoplasmic reticulum (ER), particularly the rough ER. They are involved in various important cellular processes, most notably the metabolism of xenobiotics (foreign substances) including drugs, toxins, and carcinogens.

The liver microsomes contain a variety of enzymes, such as cytochrome P450 monooxygenases, that are crucial for phase I drug metabolism. These enzymes help in the oxidation, reduction, or hydrolysis of xenobiotics, making them more water-soluble and facilitating their excretion from the body. Additionally, liver microsomes also host other enzymes involved in phase II conjugation reactions, where the metabolites from phase I are further modified by adding polar molecules like glucuronic acid, sulfate, or acetyl groups.

In summary, liver microsomes are a subcellular fraction of liver cells that play a significant role in the metabolism and detoxification of xenobiotics, contributing to the overall protection and maintenance of cellular homeostasis within the body.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

... allylisopropylacetamide MeSH D02.241.081.038.108.400 - iodoacetamide MeSH D02.241.081.038.108.650 - piracetam MeSH D02.241. ... allylisopropylacetamide MeSH D02.065.064.294 - benzeneacetamides MeSH D02.065.064.294.088 - bufexamac MeSH D02.065.064.400 - ... allylisopropylacetamide MeSH D02.455.326.271.367 - ethylenes MeSH D02.455.326.271.367.300 - dichloroethylenes MeSH D02.455. ...
"Allylisopropylacetamide" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... This graph shows the total number of publications written about "Allylisopropylacetamide" by people in this website by year, ... Below are the most recent publications written about "Allylisopropylacetamide" by people in Profiles. ... and whether "Allylisopropylacetamide" was a major or minor topic of these publications. ...
... allylisopropylacetamide MeSH D02.241.081.038.108.400 - iodoacetamide MeSH D02.241.081.038.108.650 - piracetam MeSH D02.241. ... allylisopropylacetamide MeSH D02.065.064.294 - benzeneacetamides MeSH D02.065.064.294.088 - bufexamac MeSH D02.065.064.400 - ... allylisopropylacetamide MeSH D02.455.326.271.367 - ethylenes MeSH D02.455.326.271.367.300 - dichloroethylenes MeSH D02.455. ...
Activity of Ethynyl Compounds and Conformationally Restricted and Unrestricted Analogues of Allylisopropylacetamide in Chick ...
allylisopropylacetamide. 8. 23. What 24 letter words including from letter specialtiy. Word. Scrabble Lookup-id points. Words ...
allylisopropylacetamide Any allyl isopropyl derivative of acetamide, but especially 2-propan-2-ylpent-4-enamide tha.... ... Definition and anagrams of allylisopropylacetamide. → Other senses and detailed information on the Wiktionnary ...
Tryptophan pyrrolase, tryptophan and tyrosine transaminase changes during allylisopropylacetamide-induced porphyria in the rat ...
Eggler AL, Liu G, Pezzuto JM, van Breemen RB, Mesecar AD. Modifying specific cysteines of the electrophile-sensing human Keap1 protein is insufficient to disrupt binding to the Nrf2 domain Neh2. Proc Natl Acad Sci U S A. 2005 Jul 19; 102(29):10070-5 ...
Rammes G, Seeser F, Mattusch K, Zhu K, Haas L, Kummer M, Heneka M, Herms J, Parsons CG. The NMDA receptor antagonist Radiprodil reverses the synaptotoxic effects of different amyloid-beta (A?) species on long-term potentiation (LTP). Neuropharmacology. 2018 09 15; 140:184-192 ...
D2.705.429.500.100 Allylisopropylacetamide D2.241.81.38.108.189 D2.241.81.18.110.189 American Samoa Z1.782.815.800.100 Z1.639. ...
D2.705.429.500.100 Allylisopropylacetamide D2.241.81.38.108.189 D2.241.81.18.110.189 American Samoa Z1.782.815.800.100 Z1.639. ...
D2.705.429.500.100 Allylisopropylacetamide D2.241.81.38.108.189 D2.241.81.18.110.189 American Samoa Z1.782.815.800.100 Z1.639. ...
D2.705.429.500.100 Allylisopropylacetamide D2.241.81.38.108.189 D2.241.81.18.110.189 American Samoa Z1.782.815.800.100 Z1.639. ...
D2.705.429.500.100 Allylisopropylacetamide D2.241.81.38.108.189 D2.241.81.18.110.189 American Samoa Z1.782.815.800.100 Z1.639. ...
D2.705.429.500.100 Allylisopropylacetamide D2.241.81.38.108.189 D2.241.81.18.110.189 American Samoa Z1.782.815.800.100 Z1.639. ...
D2.705.429.500.100 Allylisopropylacetamide D2.241.81.38.108.189 D2.241.81.18.110.189 American Samoa Z1.782.815.800.100 Z1.639. ...
D2.705.429.500.100 Allylisopropylacetamide D2.241.81.38.108.189 D2.241.81.18.110.189 American Samoa Z1.782.815.800.100 Z1.639. ...
This graph shows the total number of publications written about "Iodoacetamide" by people in this website by year, and whether "Iodoacetamide" was a major or minor topic of these publications ...
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Allylisopropylacetamide [D02.241.081.018.110.189] * Iodoacetamide [D02.241.081.018.110.400] * Lacosamide [D02.241.081.018. ...
2-Isopropyl-4-Pentenamide use Allylisopropylacetamide 2-Isopropylmalate Synthase 2-Keto-4-Hydroxyglutarate Dehydrogenase use ...
... of the N-demethylase activity is incapable of allylisopropylacetamide turnover and insensitive to allylisopropylacetamide ... Abstract: Allylisopropylacetamide is shown to be a suicide substrate for the phenobarbital-inducible cytochromes P-450. In ... 255, 9017-9020). The 201 product molecules of cytochrome P-450-mediated turnover of allylisopropylacetamide in either the ... Title: Determination of partition ratios for allylisopropylacetamide during suicidal processing by a phenobarbital-induced ...
D2.705.429.500.100 Allylisopropylacetamide D2.241.81.38.108.189 D2.241.81.18.110.189 American Samoa Z1.782.815.800.100 Z1.639. ...
Allylisopropylacetamide Preferred Term Term UI T001472. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1973). ... Allylisopropylacetamide Preferred Concept UI. M0000754. Registry Number. 299-78-5. Scope Note. An allylic compound that acts as ... Allylisopropylacetamide. Tree Number(s). D02.065.064.189. D02.241.081.018.110.189. D02.455.326.271.122.272. Unique ID. D000502 ...
Allylisopropylacetamide Preferred Term Term UI T001472. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1973). ... Allylisopropylacetamide Preferred Concept UI. M0000754. Registry Number. 299-78-5. Scope Note. An allylic compound that acts as ... Allylisopropylacetamide. Tree Number(s). D02.065.064.189. D02.241.081.018.110.189. D02.455.326.271.122.272. Unique ID. D000502 ...
... chemicals such as allylisopropylacetamide and 3,5-dicarbethoxy-1,4-dihydrocollidine, and natural steroids such as ...
Allylisopropylacetamide - Preferred Concept UI. M0000754. Scope note. An allylic compound that acts as a suicide inactivator of ...
In cerebellum, a diminution was observed after acute Enflurane and Isoflurane and allylisopropylacetamide, while ethanol ... Glutamatergic system; N-methyl-diethyl-aspartate; Porphyric neuropathy; Porphyrinogenic agents; allylisopropylacetamide; ...
Allyl Compounds N0000007522 Allylamine N0000167406 Allylestrenol N0000170215 Allylglycine N0000166890 Allylisopropylacetamide ...
D2.705.429.500.100 Allylisopropylacetamide D2.241.81.38.108.189 D2.241.81.18.110.189 American Samoa Z1.782.815.800.100 Z1.639. ...
D2.705.429.500.100 Allylisopropylacetamide D2.241.81.38.108.189 D2.241.81.18.110.189 American Samoa Z1.782.815.800.100 Z1.639. ...
D2.705.429.500.100 Allylisopropylacetamide D2.241.81.38.108.189 D2.241.81.18.110.189 American Samoa Z1.782.815.800.100 Z1.639. ...
D2.705.429.500.100 Allylisopropylacetamide D2.241.81.38.108.189 D2.241.81.18.110.189 American Samoa Z1.782.815.800.100 Z1.639. ...
D2.705.429.500.100 Allylisopropylacetamide D2.241.81.38.108.189 D2.241.81.18.110.189 American Samoa Z1.782.815.800.100 Z1.639. ...
... blocked by the use of allylisopropylacetamide administered intraperitoneally to rats. When synthesis was blocked, activity of ...
Allylisopropylacetamide Almanacs Almanacs as Topic Almitrine Almshouses Alnus Alocasia Aloe Alopecia Alopecia Areata Alouatta ...
  • The 201 product molecules of cytochrome P-450-mediated turnover of allylisopropylacetamide in either the microsomal or purified enzyme system are probably the epoxide, are reactive toward alkylation of cellular nucleophiles, and covalently modify protein and exogenous calf thymus DNA molecules. (nih.gov)