Carboxylesterase is a serine-dependent esterase with wide substrate specificity. The enzyme is involved in the detoxification of XENOBIOTICS and the activation of ester and of amide PRODRUGS.
Enzymes which catalyze the hydrolysis of carboxylic acid esters with the formation of an alcohol and a carboxylic acid anion.
An organophosphate cholinesterase inhibitor that is used as a pesticide.
A compound that, on administration, must undergo chemical conversion by metabolic processes before becoming the pharmacologically active drug for which it is a prodrug.
Esterases are hydrolase enzymes that catalyze the hydrolysis of ester bonds, converting esters into alcohols and acids, playing crucial roles in various biological processes including metabolism and detoxification.
The process of cleaving a chemical compound by the addition of a molecule of water.
An enzyme inhibitor that inactivates IRC-50 arvin, subtilisin, and the fatty acid synthetase complex.
A di-isopropyl-fluorophosphate which is an irreversible cholinesterase inhibitor used to investigate the NERVOUS SYSTEM.
An alkaloid isolated from the stem wood of the Chinese tree, Camptotheca acuminata. This compound selectively inhibits the nuclear enzyme DNA TOPOISOMERASES, TYPE I. Several semisynthetic analogs of camptothecin have demonstrated antitumor activity.
Enzyme catalyzing reversibly the hydrolysis of palmitoyl-CoA or other long-chain acyl coenzyme A compounds to yield CoA and palmitate or other acyl esters. The enzyme is involved in the esterification of fatty acids to form triglycerides. EC 3.1.2.2.
Nitrophenols are organic compounds characterized by the presence of a nitro group (-NO2) attached to a phenol molecule, known for their potential use in chemical and pharmaceutical industries, but also recognized as environmental pollutants due to their toxicity and potential carcinogenicity.
A wide spectrum aliphatic organophosphate insecticide widely used for both domestic and commercial agricultural purposes.
Cyclic amide of caproic acid used in manufacture of synthetic fibers of the polyamide type. Can cause local irritation.
Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.
An organothiophosphorus cholinesterase inhibitor that is used as an insecticide and as a acaricide.
The active insecticidal constituent of CHRYSANTHEMUM CINERARIIFOLIUM flowers. Pyrethrin I is the pyretholone ester of chrysanthemummonocarboxylic acid and pyrethrin II is the pyretholone ester of chrysanthemumdicarboxylic acid monomethyl ester.
7-Hydroxycoumarins. Substances present in many plants, especially umbelliferae. Umbelliferones are used in sunscreen preparations and may be mutagenic. Their derivatives are used in liver therapy, as reagents, plant growth factors, sunscreens, insecticides, parasiticides, choleretics, spasmolytics, etc.
Agents obtained from higher plants that have demonstrable cytostatic or antineoplastic activity.
Chemicals that are used to cause the disturbance, disease, or death of humans during WARFARE.
The development by insects of resistance to insecticides.
An organophosphorus compound that inhibits cholinesterase. It causes seizures and has been used as a chemical warfare agent.
Carbon-containing phosphoric acid derivatives. Included under this heading are compounds that have CARBON atoms bound to one or more OXYGEN atoms of the P(=O)(O)3 structure. Note that several specific classes of endogenous phosphorus-containing compounds such as NUCLEOTIDES; PHOSPHOLIPIDS; and PHOSPHOPROTEINS are listed elsewhere.
Naphthalene derivatives containing the -CH2CCO2H radical at the 1-position, the 2-position, or both. Compounds are used as plant growth regulators to delay sprouting, exert weed control, thin fruit, etc.
An aspect of cholinesterase (EC 3.1.1.8).
An enzyme that catalyzes reversibly the hydrolysis of acetyl-CoA to yield CoA and acetate. The enzyme is involved in the oxidation of fatty acids. EC 3.1.2.1.
An organothiophosphate cholinesterase inhibitor that is used as an insecticide and as an acaricide.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
A genus of GRAM-POSITIVE ENDOSPORE-FORMING RODS, in the family Alicyclobacillaceae, containing a unique lipid in their membranes.
Antineoplastic agent that is also used as a veterinary anesthetic. It has also been used as an intermediate in organic synthesis. Urethane is suspected to be a carcinogen.
"Esters are organic compounds that result from the reaction between an alcohol and a carboxylic acid, playing significant roles in various biological processes and often used in pharmaceutical synthesis."
An enzyme that catalyzes the hydrolysis of glycerol monoesters of long-chain fatty acids EC 3.1.1.23.
Drugs that inhibit cholinesterases. The neurotransmitter ACETYLCHOLINE is rapidly hydrolyzed, and thereby inactivated, by cholinesterases. When cholinesterases are inhibited, the action of endogenously released acetylcholine at cholinergic synapses is potentiated. Cholinesterase inhibitors are widely used clinically for their potentiation of cholinergic inputs to the gastrointestinal tract and urinary bladder, the eye, and skeletal muscles; they are also used for their effects on the heart and the central nervous system.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
Salts and esters of CHOLIC ACID.
The chemical alteration of an exogenous substance by or in a biological system. The alteration may inactivate the compound or it may result in the production of an active metabolite of an inactive parent compound. The alterations may be divided into METABOLIC DETOXICATION, PHASE I and METABOLIC DETOXICATION, PHASE II.
Pesticides designed to control insects that are harmful to man. The insects may be directly harmful, as those acting as disease vectors, or indirectly harmful, as destroyers of crops, food products, or textile fabrics.
Hydroxylated benzoic acid derivatives that contain mercury. Some of these are used as sulfhydryl reagents in biochemical studies.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
One of the long-acting synthetic ANTIDIARRHEALS; it is not significantly absorbed from the gut, and has no effect on the adrenergic system or central nervous system, but may antagonize histamine and interfere with acetylcholine release locally.
A species of gram-negative, obligately aerobic rods. Motility occurs by peritrichous flagella. (From Bergey's Manual of Determinative Bacteriology, 9th ed)
An enzyme that catalyzes the hydrolysis of ACETYLCHOLINE to CHOLINE and acetate. In the CNS, this enzyme plays a role in the function of peripheral neuromuscular junctions. EC 3.1.1.7.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Organic compounds that contain phosphorus as an integral part of the molecule. Included under this heading is broad array of synthetic compounds that are used as PESTICIDES and DRUGS.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
Any member of the class of enzymes that catalyze the cleavage of the substrate and the addition of water to the resulting molecules, e.g., ESTERASES, glycosidases (GLYCOSIDE HYDROLASES), lipases, NUCLEOTIDASES, peptidases (PEPTIDE HYDROLASES), and phosphatases (PHOSPHORIC MONOESTER HYDROLASES). EC 3.

Localization of a candidate surfactant convertase to type II cells, macrophages, and surfactant subfractions. (1/410)

Pulmonary surfactant exists in the alveolus in several distinct subtypes that differ in their morphology, composition, and surface activity. Experiments by others have implicated a serine hydrolase in the production of the inactive small vesicular subtype of surfactant (N. J. Gross and R. M. Schultz. Biochim. Biophys. Acta 1044: 222-230, 1990). Our laboratory recently identified this enzyme in the rat as the serine carboxylesterase ES-2 [F. Barr, H. Clark, and S. Hawgood. Am. J. Physiol. 274 (Lung Cell. Mol. Physiol. 18): L404-L410, 1998]. In the present study, we determined the cellular sites of expression of ES-2 in rat lung using a digoxygenin-labeled ES-2 riboprobe. ES-2 mRNA was localized to type II cells and alveolar macrophages but not to Clara cells. Using a specific ES-2 antibody, we determined the protein distribution of ES-2 in the lung by immunohistochemistry, and it was found to be consistent with the sites of mRNA expression. Most of the ES-2 in rat bronchoalveolar lavage is in the surfactant-depleted supernatant, but ES-2 was also consistently localized to the small vesicular surfactant subfraction presumed to form as a consequence of conversion activity. These results are consistent with a role for endogenous lung ES-2 in surfactant metabolism.  (+info)

Comparison of activation of CPT-11 by rabbit and human carboxylesterases for use in enzyme/prodrug therapy. (2/410)

Several recent studies have examined the possibility of producing tumor-specific cytotoxicity with various enzyme/ prodrug combinations. The enzymes are targeted to tumor cells either with antibodies (ADEPT, antibody directed enzyme prodrug therapy) or with viruses (VDEPT). The goal of the present study was to identify an appropriate enzyme for use in activating the prodrug 7-ethyl-10-[4-(1-piper-idino)-1-piperidino]carbonyloxycamptothe cin (CPT-11). In this study, we compared the efficiency of CPT-11 metabolism by rabbit and human carboxylesterases in in vitro and in situ assays. Although the rabbit and human enzymes are very similar (81% identical; 86% homologous) and the active site amino acids are 100% identical, the rabbit enzyme was 100-1000-fold more efficient at converting CPT-11 to SN-38 in vitro and was 12-55-fold more efficient in sensitizing transfected cells to CPT-11. In vivo, Rh30 rhabdomyosarcoma cells expressing the rabbit carboxylesterase and grown as xenografts in immune-deprived mice were also more sensitive to CPT-11 than were control xenografts or xenografts expressing the human enzyme. Each of the three types of xenografts regressed when the mice were treated with CPT-11 given i.v. at 2.5 mg of CPT-11/kg/daily for 5 days/week for 2 weeks [(dx5)2] (one cycle of therapy), repeated every 21 days for a total of three cycles. However, following cessation of treatment, recurrent tumors were detected in seven of seven mice bearing control Rh30 xenografts and in two of seven mice bearing Rh30 xenografts that expressed the human enzyme. No tumors recurred in mice bearing xenografts that expressed the rabbit carboxylesterase. We conclude that rabbit carboxylesterase/CPT-11 may be a useful enzyme/prodrug combination.  (+info)

Relationship between amount of esterase and gene copy number in insecticide-resistant Myzus persicae (Sulzer). (3/410)

Overproduction of the insecticide-degrading esterases, E4 and FE4, in peach-potato aphids, Myzus persicae (Sulzer), depends on both gene amplification and transcriptional control, the latter being associated with changes in DNA methylation. The structure and function of the aphid esterase genes have been studied but the determination of their copy number has proved difficult, a common problem with gene amplification. We have now used a combination of pulsed-field gel electrophoresis and quantitative competitive PCR to determine relative esterase gene copy numbers in aphid clones with different levels of insecticide resistance (R1, R2 and R3). There are approx. 4-fold increases between susceptible, R1, R2 and R3 aphids, reaching a maximum of approx. 80 times more genes in R3; this gives proportionate increases in esterase protein relative to susceptible aphids. Thus there is no overexpression of the amplified genes, in contrast with what was thought previously. For E4 genes, the loss of 5-methylcytosine is correlated with a loss of expression, greatly decreasing the amount of enzyme relative to the copy number.  (+info)

Establishment of an activated macrophage cell line, A-THP-1, and its properties. (4/410)

A new macrophage cell line with activated character and unique morphology was isolated by selecting adherent cells from the human monocytic cell line THP-1. The original THP-1 cells had been cultured for more than 9 years using 25 cm2 flasks, when cells with a different morphology appeared, adhering to the bottoms of the culture flasks. These were selected by discarding floating nonadherent cells at every subculture. Enrichment of adherent THP-1 cells with long processes proceeded during the cultivation. These adherent THP-1 showed remarkable phenotypic changes, not only morphologically, but also functionally. Namely, increased phagocytic activity, HLA-DR expression and MLR stimulator activity were remarkable. This adherent cell line was designated as activated-THP-1 (A-THP-1), since it demonstrated characteristics of activated macrophages continuously without exogenous stimulation. A cloned A-THP-1 cell line (A-THP-1 C1) also showed the same features and contained about 10% multinucleated giant cells probably caused by cell fusion. This A-THP-1 cell line, the first activated macrophage cell line to be established, provides a good model for understanding of activation mechanisms of macrophages and multinucleation. In this paper, morphological, immunological, and biological characters of this cell line are described.  (+info)

Targeting proteins to the lumen of endoplasmic reticulum using N-terminal domains of 11beta-hydroxysteroid dehydrogenase and the 50-kDa esterase. (5/410)

Previous studies identified two intrinsic endoplasmic reticulum (ER) proteins, 11beta-hydroxysteroid dehydrogenase, isozyme 1 (11beta-HSD) and the 50-kDa esterase (E3), sharing some amino acid sequence motifs in their N-terminal transmembrane (TM) domains. Both are type II membrane proteins with the C terminus projecting into the lumen of the ER. This finding implied that the N-terminal TM domains of 11beta-HSD and E3 may constitute a lumenal targeting signal (LTS). To investigate this hypothesis we created chimeric fusions using the putative targeting sequences and the reporter gene, Aequorea victoria green fluorescent protein. Transfected COS cells expressing LTS-green fluorescent protein chimeras were examined by fluorescent microscopy and electron microscopic immunogold labeling. The orientation of expressed chimeras was established by immunocytofluorescent staining of selectively permeabilized COS cells. In addition, protease protection assays of membranes in the presence and absence of detergents was used to confirm lumenal or the cytosolic orientation of the constructed chimeras. To investigate the general applicability of the proposed LTS, we fused the N terminus of E3 to the N terminus of the NADH-cytochrome b5 reductase lacking the myristoyl group and N-terminal 30-residue membrane anchor. The orientation of the cytochrome b5 reductase was reversed, from cytosolic to lumenal projection of the active domain. These observations establish that an amino acid sequence consisting of short basic or neutral residues at the N terminus, followed by a specific array of hydrophobic residues terminating with acidic residues, is sufficient for lumenal targeting of single-pass proteins that are structurally and functionally unrelated.  (+info)

Inactivation and loss of antigenicity of esterase by sugars and a steroid. (6/410)

Glycation, the non-enzymic reaction of sugars with proteins, has an important role in the complications of diabetes. It has been studied mostly in structural proteins but more recently has been shown to inactivate enzymes. Previous evidence from our laboratory indicated that glycation-induced inactivation and loss of antigenicity of catalase and superoxide dismutase are simultaneous. Esterase, which decreases activity in the lens in senile cataract and diabetes, was measured by a spectrophotometric assay using p-nitrophenyl acetate as the substrate. Here we investigated the inactivation of carboxylesterase (EC 3.1.1.1) by sugars of different glycating power and prednisolone-21-hemisuccinate while simultaneously monitoring the loss of antigenicity. Antigenicity was assessed by immunoprecipitation and by dot-blotting the glycated and non-glycated fractions of enzymes separated by affinity chromatography. Ribose and fructose inactivated more rapidly than glucose and glucose 6-phosphate. The esterase was progressively inactivated by prednisolone-21-hemisuccinate at a lower concentration. Activity and antigenicity were lost simultaneously. The glycated enzyme had entirely lost its antigenicity. These results further support the idea that inactivation of enzyme and loss of antigenicity are simultaneous.  (+info)

A non-AUG-defined alternative open reading frame of the intestinal carboxyl esterase mRNA generates an epitope recognized by renal cell carcinoma-reactive tumor-infiltrating lymphocytes in situ. (7/410)

A number of Ags recognized by tumor-reactive T cells have been characterized, including nonmutated gene products and a variety of epitopes shown to arise from either mutated or alternatively processed transcripts. Here, we report that the screening of a cDNA library with an HLA-B7-restricted renal cell carcinoma-reactive T cell clone derived from tumor-infiltrating lymphocytes (TILs) that were clonally amplified in vivo (as assessed by TCRBV complementarity determining region-3 length distribution analysis) resulted in the isolation of a nonamer encoded by an alternative open reading frame (ORF) (a +1 frameshift) of the intestinal carboxyl esterase gene. This peptide binds HLA-B*0702-presenting molecules as assessed in an immunofluorescence-based peptide binding assay using transfected T2 cells. Constitutive expression of this alternative ORF protein was observed in all transformed HLA-B7+ renal cell lines that were recognized in cytotoxicity assays by the TILs. The intestinal carboxyl esterase gene is transcribed in renal cell carcinoma tumors as well as in normal liver, intestinal, or renal tissues. Mutation of the natural ATG translation initiation site did not alter recognition, indicating that frameshifting (i.e., slippage of the ribosome forward) and recoding are not involved. In addition, a point mutation of the three AUG codons that may be used as alternative translation initiation sites in the +1 ORF did not abolish recognition, whereas mutation of an upstream ACG codon did, indicating that the latter codon initiates the translation of the alternative ORF. These results further extend the types of Ags that can be recognized by tumor-reactive TILs in situ (i.e., leading to clonal T cell expansion).  (+info)

Microsomal long-chain acyl-CoA thioesterase (carboxylesterase ES-4) is regulated by thyroxine. (8/410)

Long chain acyl-CoA thioesterase activity is mainly located in microsomes after subcellular fractionation of liver from untreated rats. The physiological function and regulation of expression of this activity is not known. In the present study we have investigated the effect of thyroxine on expression of carboxylesterase ES-4, the major acyl-CoA thioesterase of liver microsomes. Thyroidectomy of rats decreased the palmitoyl-CoA thioesterase activity to about 25% of normal activity. This decrease was accompanied by similar decreases at the protein and mRNA levels (31% and 57%, respectively, of controls). Treatment with thyroxine completely reversed the effect of thyroidectomy and resulted in elevated levels in both thyroidectomized and control rats. For reasons of comparison we also studied the possibility that ES-10 and ES-2, two other members of the same gene family, are affected by thyroxine. ES-10 was not changed at the protein or mRNA level by any of the treatments, while ES-2 expression in liver was decreased by thyroxine treatment. The data shows that changes in activity and expression of ES-4 correlate to thyroxine status in the rat suggesting a physiological regulatory role by this hormone. Since thyroxine regulates the expression of lipogenic enzymes, these results are consistent with a function for this microsomal acyl-CoA thioesterase in fatty acid synthesis and/or secretion, rather than in oxidative degradation of fatty acids.  (+info)

Carboxylesterase is a type of enzyme that catalyzes the hydrolysis of ester bonds in carboxylic acid esters, producing alcohol and carboxylate products. These enzymes are widely distributed in various tissues, including the liver, intestines, and plasma. They play important roles in detoxification, metabolism, and the breakdown of xenobiotics (foreign substances) in the body.

Carboxylesterases can also catalyze the reverse reaction, forming esters from alcohols and carboxylates, which is known as transesterification or esterification. This activity has applications in industrial processes and biotechnology.

There are several families of carboxylesterases, with different substrate specificities, kinetic properties, and tissue distributions. These enzymes have been studied for their potential use in therapeutics, diagnostics, and drug delivery systems.

Carboxylic ester hydrolases are a class of enzymes that catalyze the hydrolysis of ester bonds in carboxylic acid esters, producing alcohols and carboxylates. This group includes several subclasses of enzymes such as esterases, lipases, and thioesterases. These enzymes play important roles in various biological processes, including metabolism, detoxification, and signal transduction. They are widely used in industrial applications, such as the production of biodiesel, pharmaceuticals, and food ingredients.

Paraoxon is the active metabolite of the organophosphate insecticide parathion. It functions as an acetylcholinesterase inhibitor, which means it prevents the breakdown of the neurotransmitter acetylcholine in the synaptic cleft. This leads to an accumulation of acetylcholine and overstimulation of cholinergic receptors, causing a variety of symptoms such as muscle weakness, increased salivation, sweating, lacrimation, nausea, vomiting, and potentially fatal respiratory failure.

Paraoxon is also used in research and diagnostic settings to measure acetylcholinesterase activity. It can be used to determine the degree of inhibition of this enzyme by various chemicals or toxins, including other organophosphate compounds.

A prodrug is a pharmacologically inactive substance that, once administered, is metabolized into a drug that is active. Prodrugs are designed to improve the bioavailability or delivery of a drug, to minimize adverse effects, or to target the drug to specific sites in the body. The conversion of a prodrug to its active form typically occurs through enzymatic reactions in the liver or other tissues.

Prodrugs can offer several advantages over traditional drugs, including:

* Improved absorption: Some drugs have poor bioavailability due to their chemical properties, which make them difficult to absorb from the gastrointestinal tract. Prodrugs can be designed with improved absorption characteristics, allowing for more efficient delivery of the active drug to the body.
* Reduced toxicity: By masking the active drug's chemical structure, prodrugs can reduce its interactions with sensitive tissues and organs, thereby minimizing adverse effects.
* Targeted delivery: Prodrugs can be designed to selectively release the active drug in specific areas of the body, such as tumors or sites of infection, allowing for more precise and effective therapy.

Examples of prodrugs include:

* Aspirin (acetylsalicylic acid), which is metabolized to salicylic acid in the liver.
* Enalapril, an angiotensin-converting enzyme (ACE) inhibitor used to treat hypertension and heart failure, which is metabolized to enalaprilat in the liver.
* Codeine, an opioid analgesic, which is metabolized to morphine in the liver by the enzyme CYP2D6.

It's important to note that not all prodrugs are successful, and some may even have unintended consequences. For example, if a patient has a genetic variation that affects the activity of the enzyme responsible for converting the prodrug to its active form, the drug may not be effective or may produce adverse effects. Therefore, it's essential to consider individual genetic factors when prescribing prodrugs.

Esterases are a group of enzymes that catalyze the hydrolysis of ester bonds in esters, producing alcohols and carboxylic acids. They are widely distributed in plants, animals, and microorganisms and play important roles in various biological processes, such as metabolism, digestion, and detoxification.

Esterases can be classified into several types based on their substrate specificity, including carboxylesterases, cholinesterases, lipases, and phosphatases. These enzymes have different structures and mechanisms of action but all share the ability to hydrolyze esters.

Carboxylesterases are the most abundant and diverse group of esterases, with a wide range of substrate specificity. They play important roles in the metabolism of drugs, xenobiotics, and lipids. Cholinesterases, on the other hand, specifically hydrolyze choline esters, such as acetylcholine, which is an important neurotransmitter in the nervous system. Lipases are a type of esterase that preferentially hydrolyzes triglycerides and plays a crucial role in fat digestion and metabolism. Phosphatases are enzymes that remove phosphate groups from various molecules, including esters, and have important functions in signal transduction and other cellular processes.

Esterases can also be used in industrial applications, such as in the production of biodiesel, detergents, and food additives. They are often produced by microbial fermentation or extracted from plants and animals. The use of esterases in biotechnology is an active area of research, with potential applications in biofuel production, bioremediation, and medical diagnostics.

Hydrolysis is a chemical process, not a medical one. However, it is relevant to medicine and biology.

Hydrolysis is the breakdown of a chemical compound due to its reaction with water, often resulting in the formation of two or more simpler compounds. In the context of physiology and medicine, hydrolysis is a crucial process in various biological reactions, such as the digestion of food molecules like proteins, carbohydrates, and fats. Enzymes called hydrolases catalyze these hydrolysis reactions to speed up the breakdown process in the body.

Phenylmethylsulfonyl Fluoride (PMSF) is not a medication or a treatment, but it is a chemical compound with the formula C8H9FO3S. It is commonly used in biochemistry and molecular biology research as a serine protease inhibitor.

Proteases are enzymes that break down other proteins by cleaving specific peptide bonds. Serine proteases are a class of proteases that use a serine residue in their active site to carry out the hydrolysis reaction. PMSF works by irreversibly modifying this serine residue, inhibiting the enzyme's activity.

PMSF is used in laboratory settings to prevent protein degradation during experiments such as protein purification or Western blotting. It is important to note that PMSF is highly toxic and must be handled with care, using appropriate personal protective equipment (PPE) and safety measures.

I'm sorry for any confusion, but "Isoflurophate" does not appear to be a recognized term in medical or scientific literature. It is possible that there may be a spelling error or typo in the term you are looking for. If you meant "Isoflurane," which is a commonly used anesthetic in medical and surgical procedures, I can provide a definition for that.

Isoflurane: A volatile halogenated ether liquid used as an inhalational general anesthetic agent. It has a rapid onset and offset of action, making it useful for both induction and maintenance of anesthesia. Isoflurane is also known to have bronchodilatory properties, which can be beneficial in patients with reactive airway disease or asthma.

Camptothecin is a topoisomerase I inhibitor, which is a type of chemotherapeutic agent used in cancer treatment. It works by interfering with the function of an enzyme called topoisomerase I, which helps to uncoil DNA during cell division. By inhibiting this enzyme, camptothecin prevents the cancer cells from dividing and growing, ultimately leading to their death.

Camptothecin is found naturally in the bark and stem of the Camptotheca acuminata tree, also known as the "happy tree," which is native to China. It was first isolated in 1966 and has since been developed into several synthetic derivatives, including irinotecan and topotecan, which are used clinically to treat various types of cancer, such as colon, lung, and ovarian cancers.

Like other chemotherapeutic agents, camptothecin can have significant side effects, including nausea, vomiting, diarrhea, and myelosuppression (suppression of bone marrow function). It is important for patients receiving camptothecin-based therapies to be closely monitored by their healthcare team to manage these side effects effectively.

Palmitoyl-CoA hydrolase is an enzyme that catalyzes the hydrolysis of palmitoyl-coenzyme A (palmitoyl-CoA) to produce free coenzyme A (CoA) and palmitic acid. Palmitoyl-CoA is a fatty acyl-CoA ester that plays a central role in lipid metabolism, particularly in the synthesis of complex lipids such as triacylglycerols and phospholipids.

The reaction catalyzed by palmitoyl-CoA hydrolase is:

palmitoyl-CoA + H2O → CoA + palmitic acid

This enzyme is important for regulating the levels of palmitoyl-CoA in cells and may play a role in the development of metabolic disorders such as obesity and non-alcoholic fatty liver disease. Palmitoyl-CoA hydrolase has also been studied as a potential target for the development of therapies to treat these conditions.

Nitrophenols are organic compounds that contain a hydroxyl group (-OH) attached to a phenyl ring (aromatic hydrocarbon) and one or more nitro groups (-NO2). They have the general structure R-C6H4-NO2, where R represents the hydroxyl group.

Nitrophenols are known for their distinctive yellow to brown color and can be found in various natural sources such as plants and microorganisms. Some common nitrophenols include:

* p-Nitrophenol (4-nitrophenol)
* o-Nitrophenol (2-nitrophenol)
* m-Nitrophenol (3-nitrophenol)

These compounds are used in various industrial applications, including dyes, pharmaceuticals, and agrochemicals. However, they can also be harmful to human health and the environment, as some nitrophenols have been identified as potential environmental pollutants and may pose risks to human health upon exposure.

Malathion is a type of organophosphate pesticide that is widely used in agriculture, public health, and residential settings for the control of various insect pests. It works by inhibiting an enzyme called acetylcholinesterase, which leads to the accumulation of the neurotransmitter acetylcholine in the synapses, resulting in overstimulation of the nervous system and ultimately death of the insect.

In a medical context, malathion is also used as a topical treatment for head lice infestations. It is available in various forms, such as shampoos, lotions, and sprays, and works by killing the lice and their eggs on contact. However, it is important to follow the instructions carefully when using malathion products to avoid excessive exposure and potential health risks.

Caprolactam is a chemical compound with the formula (CH2)5CNH. It is a white solid that is used in the industrial synthesis of nylon-6, a type of polyamide. Caprolactam is produced from cyclohexanone and ammonia in a two-step process: first, cyclohexanone oxime is formed, which is then converted to caprolactam through a Beckmann rearrangement.

Caprolactam has a six-membered ring structure with an amide functional group. It is a versatile intermediate in the chemical industry and is also used in the production of other polymers, resins, and pharmaceuticals. Caprolactam is not naturally occurring and is produced through chemical synthesis.

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.

Pyrethrins are a group of naturally occurring organic compounds extracted from the flowers of Chrysanthemum cinerariaefolium and Chrysanthemum coccineum. They have been used for centuries as insecticides due to their ability to disrupt the nervous system of insects, leading to paralysis and death. Pyrethrins are composed of six esters, pyrethrin I and II, cinerin I and II, and jasmolin I and II, which have different insecticidal properties but share a similar mode of action. They are commonly used in household insect sprays, pet shampoos, and agricultural applications to control a wide range of pests. However, pyrethrins can be toxic to fish and some beneficial insects, so they must be used with caution.

Umbelliferone is not a medical term, but a chemical compound that belongs to the class of coumarins. It can be found in various plants, including those from the family Apiaceae (also known as Umbelliferae), hence its name. Coumarins like umbelliferone have been studied for their potential pharmacological properties, such as anticoagulant, anti-inflammatory, and antimicrobial activities. However, they are not typically considered as a medical treatment on their own.

Antineoplastic agents, phytogenic, also known as plant-derived anticancer drugs, are medications that are derived from plants and used to treat cancer. These agents have natural origins and work by interfering with the growth and multiplication of cancer cells, helping to slow or stop the spread of the disease. Some examples of antineoplastic agents, phytogenic include paclitaxel (Taxol), vincristine, vinblastine, and etoposide. These drugs are often used in combination with other treatments such as surgery, radiation therapy, and other medications to provide a comprehensive approach to cancer care.

Chemical warfare agents are defined as chemical substances that are intended or have the capability to cause death, injury, temporary incapacitation, or sensory irritation through their toxic properties when deployed in a military theater. These agents can be in gaseous, liquid, or solid form and are typically categorized based on their physiological effects. Common categories include nerve agents (e.g., sarin, VX), blister agents (e.g., mustard gas), choking agents (e.g., phosgene), blood agents (e.g., cyanide), and incapacitating agents (e.g., BZ). The use of chemical warfare agents is prohibited by international law under the Chemical Weapons Convention.

Insecticide resistance is a genetic selection process in insect populations that allows them to survive and reproduce despite exposure to insecticides. It's the result of changes in the genetic makeup of insects, which can be caused by natural selection when insecticides are used repeatedly. Over time, this leads to the prevalence of genes that provide resistance to the insecticide, making the pest control methods less effective. Insecticide resistance is a significant challenge in public health and agriculture, as it can reduce the efficacy of interventions aimed at controlling disease-carrying insects or protecting crops from pests.

Soman is a chemical compound with the formula (CH3)2(C=O)N(CH2)4SH. It is a potent nerve agent, a type of organic compound that can cause death by interfering with the nervous system's ability to regulate muscle movement. Soman is an odorless, colorless liquid that evaporates slowly at room temperature and is therefore classified as a "v-type" or "volatile" nerve agent. It is considered to be one of the most toxic substances known. Exposure to soman can occur through inhalation, skin contact, or ingestion, and it can cause a range of symptoms including nausea, seizures, respiratory failure, and death.

Organophosphates are a group of chemicals that include insecticides, herbicides, and nerve gases. They work by inhibiting an enzyme called acetylcholinesterase, which normally breaks down the neurotransmitter acetylcholine in the synapse between nerves. This leads to an overaccumulation of acetylcholine, causing overstimulation of the nervous system and resulting in a wide range of symptoms such as muscle twitching, nausea, vomiting, diarrhea, sweating, confusion, and potentially death due to respiratory failure. Organophosphates are highly toxic and their use is regulated due to the risks they pose to human health and the environment.

Naphthaleneacetic acids (NAAs) are a type of synthetic auxin, which is a plant hormone that promotes growth and development. Specifically, NAAs are derivatives of naphthalene, a polycyclic aromatic hydrocarbon, with a carboxylic acid group attached to one of the carbon atoms in the ring structure.

NAAs are commonly used in horticulture and agriculture as plant growth regulators. They can stimulate rooting in cuttings, promote fruit set and growth, and inhibit vegetative growth. NAAs can also be used in plant tissue culture to regulate cell division and differentiation.

In medical terms, NAAs are not typically used as therapeutic agents. However, they have been studied for their potential use in cancer therapy due to their ability to regulate cell growth and differentiation. Some research has suggested that NAAs may be able to inhibit the growth of certain types of cancer cells, although more studies are needed to confirm these findings and determine the safety and efficacy of NAAs as a cancer treatment.

Butyrylcholinesterase (BChE) is an enzyme that catalyzes the hydrolysis of esters of choline, including butyrylcholine and acetylcholine. It is found in various tissues throughout the body, including the liver, brain, and plasma. BChE plays a role in the metabolism of certain drugs and neurotransmitters, and its activity can be inhibited by certain chemicals, such as organophosphate pesticides and nerve agents. Elevated levels of BChE have been found in some neurological disorders, while decreased levels have been associated with genetic deficiencies and liver disease.

Acetyl-CoA hydrolase is an enzyme that catalyzes the hydrolysis of Acetyl-CoA into acetate and coenzyme A (CoA). The chemical reaction it catalyzes is as follows:

Acetyl-CoA + H2O → acetate + CoA-SH

This enzyme plays a role in the metabolism of fatty acids, cholesterol, and other compounds. It is also involved in the detoxification of certain drugs and chemicals that are conjugated with Acetyl-CoA before being excreted from the body.

Acetyl-CoA hydrolase is found in various tissues, including the liver, kidney, and intestine. It belongs to the family of hydrolases, specifically those acting on thioester bonds. The gene that encodes this enzyme is called "ACOT" (Acyl-CoA thioesterase). Mutations in this gene have been associated with neurological disorders and other health conditions.

Chlorpyrifos is a type of pesticide that belongs to the class of organophosphates. It works by inhibiting the enzyme acetylcholinesterase, which leads to an accumulation of the neurotransmitter acetylcholine and causes toxic effects in insects. Chlorpyrifos is used to control a wide variety of pests, including insects that infest crops, homes, and gardens. It is also used to protect wood from termites and other wood-boring insects.

Chlorpyrifos can be harmful to humans if it is ingested, inhaled, or comes into contact with the skin. Exposure to chlorpyrifos can cause a range of symptoms, including nausea, vomiting, headache, dizziness, and muscle twitching. In severe cases, it can lead to respiratory failure, convulsions, and even death. Chlorpyrifos has been linked to developmental problems in children, including reduced IQ and attention deficit disorder. As a result, the use of chlorpyrifos in residential settings has been restricted in many countries.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Alicyclobacillus is a genus of bacteria that are characterized by their ability to produce endospores and their resistance to high temperatures. These bacteria are gram-positive, rod-shaped, and facultatively anaerobic, meaning they can grow in the presence or absence of oxygen. They are commonly found in soil, water, and food, particularly acidic foods such as fruit juices and sauces. Some species of Alicyclobacillus can produce compounds that give off a smoky or medicinal odor and taste, which can affect the quality and safety of food products.

Urethane is not a term typically used in medical definitions. However, in the field of chemistry and pharmacology, urethane is an ethyl carbamate ester which has been used as a general anesthetic. It is rarely used today due to its potential carcinogenic properties and the availability of safer alternatives.

In the context of materials science, polyurethanes are a class of polymers that contain urethane linkages (-NH-CO-O-) in their main chain. They are widely used in various applications such as foam insulation, coatings, adhesives, and medical devices due to their versatile properties like flexibility, durability, and resistance to abrasion.

Esters are organic compounds that are formed by the reaction between an alcohol and a carboxylic acid. They are widely found in nature and are used in various industries, including the production of perfumes, flavors, and pharmaceuticals. In the context of medical definitions, esters may be mentioned in relation to their use as excipients in medications or in discussions of organic chemistry and biochemistry. Esters can also be found in various natural substances such as fats and oils, which are triesters of glycerol and fatty acids.

Monoacylglycerol lipases (MAGLs) are a type of enzyme that play a role in the metabolism of lipids, specifically by breaking down monoacylglycerols into glycerol and free fatty acids. Monoacylglycerols are formed during the digestion of dietary fats and are also produced endogenously as a result of the breakdown of complex lipids.

MAGLs are widely distributed throughout the body, but are particularly abundant in tissues that utilize large amounts of fatty acids for energy, such as the liver, heart, and skeletal muscle. In addition to their role in lipid metabolism, MAGLs have been implicated in various physiological processes, including inflammation, pain perception, and cancer.

Inhibition of MAGL activity has been proposed as a potential therapeutic strategy for the treatment of various diseases, including obesity, diabetes, and neurodegenerative disorders. However, further research is needed to fully understand the role of MAGLs in these processes and to determine the safety and efficacy of MAGL inhibitors as drugs.

Cholinesterase inhibitors are a class of drugs that work by blocking the action of cholinesterase, an enzyme that breaks down the neurotransmitter acetylcholine in the body. By inhibiting this enzyme, the levels of acetylcholine in the brain increase, which can help to improve symptoms of cognitive decline and memory loss associated with conditions such as Alzheimer's disease and other forms of dementia.

Cholinesterase inhibitors are also used to treat other medical conditions, including myasthenia gravis, a neuromuscular disorder that causes muscle weakness, and glaucoma, a condition that affects the optic nerve and can lead to vision loss. Some examples of cholinesterase inhibitors include donepezil (Aricept), galantamine (Razadyne), and rivastigmine (Exelon).

It's important to note that while cholinesterase inhibitors can help to improve symptoms in some people with dementia, they do not cure the underlying condition or stop its progression. Side effects of these drugs may include nausea, vomiting, diarrhea, and increased salivation. In rare cases, they may also cause seizures, fainting, or cardiac arrhythmias.

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.

I'm sorry for any confusion, but "Cholates" is not a recognized medical term or abbreviation in physiology, pathology, or pharmacology. It seems like there might be a spelling mistake or a misunderstanding. If you meant to ask about "cholesterol," I would be happy to help provide information on that.

Cholesterol is a type of lipid (fat) that is essential for the normal functioning of our bodies. It plays crucial roles in maintaining cell membrane structure, producing certain hormones, and serving as a precursor for vitamin D and bile acids. However, high levels of cholesterol in the blood can increase the risk of developing cardiovascular diseases.

If you have any questions or need more information about cholesterol or any other medical topic, please feel free to ask!

Biotransformation is the metabolic modification of a chemical compound, typically a xenobiotic (a foreign chemical substance found within an living organism), by a biological system. This process often involves enzymatic conversion of the parent compound to one or more metabolites, which may be more or less active, toxic, or mutagenic than the original substance.

In the context of pharmacology and toxicology, biotransformation is an important aspect of drug metabolism and elimination from the body. The liver is the primary site of biotransformation, but other organs such as the kidneys, lungs, and gastrointestinal tract can also play a role.

Biotransformation can occur in two phases: phase I reactions involve functionalization of the parent compound through oxidation, reduction, or hydrolysis, while phase II reactions involve conjugation of the metabolite with endogenous molecules such as glucuronic acid, sulfate, or acetate to increase its water solubility and facilitate excretion.

Insecticides are substances or mixtures of substances intended for preventing, destroying, or mitigating any pest, including insects, arachnids, or other related pests. They can be chemical or biological agents that disrupt the growth, development, or behavior of these organisms, leading to their death or incapacitation. Insecticides are widely used in agriculture, public health, and residential settings for pest control. However, they must be used with caution due to potential risks to non-target organisms and the environment.

Hydroxymercuribenzoates are a group of organic compounds that contain a mercury atom bonded to a hydroxyl group and a benzene ring. They were historically used in medicine as antiseptics and preservatives, but their use has been largely discontinued due to the toxicity of mercury.

The general structure of a hydroxymercuribenzoate is R-C6H4-COOH, where R represents a mercury atom bonded to a hydroxyl group (-OH). The most common example of this class of compounds is merbromin (also known as Mercurochrome), which has the chemical formula C9H9HgNaO2S.

It's important to note that due to the toxicity of mercury, these compounds are no longer used in modern medicine and have been replaced by safer alternatives.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Loperamide is an antidiarrheal medication that works by slowing down the movement of the intestines. This helps to increase the time between bowel movements and reduces the amount of liquid in stools, thereby helping to relieve diarrhea. It is available over-the-counter (OTC) and by prescription, depending on the strength and formulation.

Loperamide works by binding to opioid receptors in the gut, which helps to reduce the contractions of the intestines that can lead to diarrhea. It is important to note that loperamide should not be used for longer than 2 days without consulting a healthcare professional, as prolonged use can lead to serious side effects such as constipation, dizziness, and decreased alertness.

Loperamide is also known by its brand names, including Imodium, Pepto-Bismol Maximum Strength, and Kaopectate II. It is important to follow the instructions on the label carefully when taking loperamide, and to speak with a healthcare provider if you have any questions or concerns about using this medication.

"Ochrobactrum anthropi" is a gram-negative, rod-shaped bacterium that is found in various environments, including soil, water, and clinical samples. It is a conditional pathogen, meaning it can cause infection under certain circumstances, particularly in immunocompromised individuals. Infections caused by Ochrobactrum anthropi are often associated with medical devices or procedures, such as catheter-related bacteremia, pneumonia, and wound infections. It is inherently resistant to many antibiotics, which can make treatment challenging.

Acetylcholinesterase (AChE) is an enzyme that catalyzes the hydrolysis of acetylcholine (ACh), a neurotransmitter, into choline and acetic acid. This enzyme plays a crucial role in regulating the transmission of nerve impulses across the synapse, the junction between two neurons or between a neuron and a muscle fiber.

Acetylcholinesterase is located in the synaptic cleft, the narrow gap between the presynaptic and postsynaptic membranes. When ACh is released from the presynaptic membrane and binds to receptors on the postsynaptic membrane, it triggers a response in the target cell. Acetylcholinesterase rapidly breaks down ACh, terminating its action and allowing for rapid cycling of neurotransmission.

Inhibition of acetylcholinesterase leads to an accumulation of ACh in the synaptic cleft, prolonging its effects on the postsynaptic membrane. This can result in excessive stimulation of cholinergic receptors and overactivation of the cholinergic system, which may cause a range of symptoms, including muscle weakness, fasciculations, sweating, salivation, lacrimation, urination, defecation, bradycardia, and bronchoconstriction.

Acetylcholinesterase inhibitors are used in the treatment of various medical conditions, such as Alzheimer's disease, myasthenia gravis, and glaucoma. However, they can also be used as chemical weapons, such as nerve agents, due to their ability to disrupt the nervous system and cause severe toxicity.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Organophosphorus compounds are a class of chemical substances that contain phosphorus bonded to organic compounds. They are used in various applications, including as plasticizers, flame retardants, pesticides (insecticides, herbicides, and nerve gases), and solvents. In medicine, they are also used in the treatment of certain conditions such as glaucoma. However, organophosphorus compounds can be toxic to humans and animals, particularly those that affect the nervous system by inhibiting acetylcholinesterase, an enzyme that breaks down the neurotransmitter acetylcholine. Exposure to these compounds can cause symptoms such as nausea, vomiting, muscle weakness, and in severe cases, respiratory failure and death.

An encyclopedia is a comprehensive reference work containing articles on various topics, usually arranged in alphabetical order. In the context of medicine, a medical encyclopedia is a collection of articles that provide information about a wide range of medical topics, including diseases and conditions, treatments, tests, procedures, and anatomy and physiology. Medical encyclopedias may be published in print or electronic formats and are often used as a starting point for researching medical topics. They can provide reliable and accurate information on medical subjects, making them useful resources for healthcare professionals, students, and patients alike. Some well-known examples of medical encyclopedias include the Merck Manual and the Stedman's Medical Dictionary.

Hydrolases are a class of enzymes that help facilitate the breakdown of various types of chemical bonds through a process called hydrolysis, which involves the addition of water. These enzymes catalyze the cleavage of bonds in substrates by adding a molecule of water, leading to the formation of two or more smaller molecules.

Hydrolases play a crucial role in many biological processes, including digestion, metabolism, and detoxification. They can act on a wide range of substrates, such as proteins, lipids, carbohydrates, and nucleic acids, breaking them down into smaller units that can be more easily absorbed or utilized by the body.

Examples of hydrolases include:

1. Proteases: enzymes that break down proteins into smaller peptides or amino acids.
2. Lipases: enzymes that hydrolyze lipids, such as triglycerides, into fatty acids and glycerol.
3. Amylases: enzymes that break down complex carbohydrates, like starches, into simpler sugars, such as glucose.
4. Nucleases: enzymes that cleave nucleic acids, such as DNA or RNA, into smaller nucleotides or oligonucleotides.
5. Phosphatases: enzymes that remove phosphate groups from various substrates, including proteins and lipids.
6. Esterases: enzymes that hydrolyze ester bonds in a variety of substrates, such as those found in some drugs or neurotransmitters.

Hydrolases are essential for maintaining proper cellular function and homeostasis, and their dysregulation can contribute to various diseases and disorders.

... carboxylesterase 1 carboxylesterase 2 carboxylesterase 3 esterase A, esterase B, esterase D, methylbutyrase, methylbutyrate ... has a role as a human carboxylesterase inhibitor. The carboxylesterase family of evolutionarily related proteins (those with ... The enzyme carboxylesterase (or carboxylic-ester hydrolase, EC 3.1.1.1; systematic name carboxylic-ester hydrolase) catalyzes ... Humans genes that encode carboxylesterase enzymes include: CES1 CES2 CES3 CES4 CES7 CES8 An approved nomenclature has been ...
... is an enzyme that in humans is encoded by the CES3 gene. Carboxylesterase 3 is a member of a large multigene ... "Entrez Gene: CES3 carboxylesterase 3 (brain)". Lee CV, Hymowitz SG, Wallweber HJ, et al. (2006). "Synthetic anti-BR3 antibodies ... Aida K, Moore R, Negishi M (1993). "Cloning and nucleotide sequence of a novel, male-predominant carboxylesterase in mouse ... and a newly expressed carboxylesterase isoenzyme, CES3". Drug Metab Dispos. 32 (5): 505-11. doi:10.1124/dmd.32.5.505. PMID ...
Liver carboxylesterase 1 also known as carboxylesterase 1 (CES1, hCE-1 or CES1A1) is an enzyme that in humans is encoded by the ... Carboxylesterase 1 is a serine esterase and member of a large multigene carboxylesterase family. It is also part of the alpha/ ... "Entrez Gene: CES1 carboxylesterase 1 (monocyte/macrophage serine esterase 1)". Imai T (Jun 2006). "Human Carboxylesterase ... Carboxylesterase 1 deficiency may be associated with non-Hodgkin lymphoma or B-cell lymphocytic leukemia. Inhibition of CES1 by ...
"Entrez Gene: CES2 carboxylesterase 2 (intestine, liver)". Imai T (June 2006). "Human carboxylesterase isozymes: catalytic ... Carboxylesterase 2 is an enzyme that in humans is encoded by the CES2 gene. It is a member of the alpha/beta fold hydrolase ... Carboxylesterase 2 is a member of a large multigene family. The enzymes encoded by these genes are responsible for the ... Charasson V, Bellott R, Meynard D, Longy M, Gorry P, Robert J (December 2004). "Pharmacogenetics of human carboxylesterase 2, ...
Carboxylesterase, type B is a family of evolutionarily related proteins that belongs to the superfamily of proteins with the ... ACHE ARACHE BCHE CEL CES1 CES2 CES3 CES4 CES7 CES8 NLGN1 NLGN2 NLGN3 NLGN4X NLGN4Y TG Carboxylesterase Nachon F, Asojo OA, ... IPR000997 Human genes that encode proteins containing the carboxylesterase domain include: ...
Notum, palmitoleoyl-protein carboxylesterase is a protein that in humans is encoded by the NOTUM gene. GRCh38: Ensembl release ... "Entrez Gene: Notum, palmitoleoyl-protein carboxylesterase". Retrieved 2018-06-15. Torisu Y, Watanabe A, Nonaka A, Midorikawa Y ... provides an overview of all the structure information available in the PDB for Human Palmitoleoyl-protein carboxylesterase ...
It belongs to the carboxylesterase family of enzymes. It is the primary target of inhibition by organophosphorus compounds such ...
The hydrolysis was found to be catalyzed by carboxylesterase 1 (CES1). Etymologically, ritalinic acid shares its roots with ... August 2004). "Methylphenidate is stereoselectively hydrolyzed by human carboxylesterase CES1A1". The Journal of Pharmacology ...
August 2004). "Methylphenidate is stereoselectively hydrolyzed by human carboxylesterase CES1A1". The Journal of Pharmacology ...
Wang BZ, Guo P, Hang BJ, Li L, He J, Li SP (September 2009). "Cloning of a novel pyrethroid-hydrolyzing carboxylesterase gene ... The enzyme pyrethroid hydrolase (EC 3.1.1.88, pyrethroid-hydrolyzing carboxylesterase, pyrethroid-hydrolysing esterase, ... and purification of a pyrethroid-hydrolyzing carboxylesterase from mouse liver microsomes". The Journal of Biological Chemistry ...
... is a carboxylesterase that is excreted in large amounts in cat urine. There is also evidence that it can serve as a ... It is also the first carboxylesterase to be found in urine. Cauxin has been shown to hydrolyze 3-methylbutanol-cysteinylglycine ... "Characterisation of the carboxylesterase enzyme cauxin in the seminal fluid of the cat". The Veterinary Journal. 190 (3): 378- ... a Carboxylesterase-Like Enzyme, Is Present and Active in Mammalian Male Reproductive Fluids1". Biology of Reproduction. 74 (2 ...
Metabolism of pethidine to pethidinic acid is carried out mainly by the carboxylesterase enzyme hCE-1 in the liver, and since ... Zhang J, Burnell JC, Dumaual N, Bosron WF (July 1999). "Binding and hydrolysis of meperidine by human liver carboxylesterase ...
Moroi K, Kuga T (April 1982). "Inhibitory effect of leptophos on carboxylesterase (isocarboxazid amidase) in rat liver". ...
Cunnac S, Wilson A, Nuwer J, Kirik A, Baranage G, Mudgett MB (February 2007). "A conserved carboxylesterase is a SUPPRESSOR OF ...
Potential Regulatory Role of Human-Carboxylesterase-1 Glycosylation in Liver Cancer Cell Growth. Y., K. Paik; J., E. Graham; M ... "Human liver carboxylesterase 1 outperforms alpha-fetoprotein as biomarker to discriminate hepatocellular carcinoma from other ... "Potential Regulatory Role of Human-Carboxylesterase-1 Glycosylation in Liver Cancer Cell Growth". Journal of Proteome Research ...
In rodent models, butyl acrylate is metabolized by carboxylesterase or reactions with glutathione; this detoxification produces ...
Selim, Samy; Hagagy, Nashwa (2016-03-01). "Genome sequence of carboxylesterase, carboxylase and xylose isomerase producing ... and carboxylesterase. Other genes coding for biosynthesis of peptides and secondary metabolites were also detected. ...
Furthermore, cauxin is a carboxylesterase enzyme which hydrolyzes 3-methylbutanol-cysteinylglycine (MBCG) into felinine. Thus, ... a majority of MBCG is hydrolyzed to felinine and glycine by carboxylesterase 5A, or cauxin. Cauxin specifically works by ...
The enzyme cocaine esterase (EC 3.1.1.84, CocE, hCE2, hCE-2, human carboxylesterase 2; systematic name cocaine benzoylhydrolase ... "Purification and cloning of a broad substrate specificity human liver carboxylesterase that catalyzes the hydrolysis of cocaine ...
Thomsen R, Rasmussen HB, Linnet K (January 2014). "In vitro drug metabolism by human carboxylesterase 1: focus on angiotensin- ... Ramipril, a prodrug or precursor drug, is converted to the active metabolite ramiprilat by carboxylesterase 1. Ramiprilat is ...
Prilocaine, an amino amide-type local anesthetic, yields o-toluidine when metabolized by carboxylesterase enzymes. Large ... and Lidocaine-Induced Methemoglobinemia Is Caused by Human Carboxylesterase-, CYP2E1-, and CYP3A4-Mediated Metabolic Activation ...
... a new carboxylesterase from Escherichia coli". The Journal of Biological Chemistry. 278 (28): 26039-45. doi:10.1074/jbc. ...
"Identification of the Catalytic Residues of Carboxylesterase from by Diisopropyl Fluorophosphate-Labeling and Site-Directed ...
White KN, Hope DB (1984). "Partial purification and characterization of a microsomal carboxylesterase specific for salicylate ...
... resistance is thought to always be due to either increased carboxylesterase concentrations or altered ...
"Molecular cloning of the carboxylesterase gene and biochemical characterization of the encoded protein from Pseudomonas ...
This carboxylesterase-dependent transesterification process is also known to occur when cocaine and alcohol are consumed ... Bourland JA, Martin DK, Mayersohn M (December 1997). "Carboxylesterase-mediated transesterification of meperidine (Demerol) and ...
2013). OATP1A/1B Transporters Affect Irinotecan and SN-38 Pharmacokinetics and Carboxylesterase Expression in Knockout and ...
... while organophosphate resistance most commonly is carboxylesterase metabolization. While the carbamate acetylcholinesterase ...
August 2014). "Structural insights into the low pH adaptation of a unique carboxylesterase from Ferroplasma: altering the pH ...
... carboxylesterase 1 carboxylesterase 2 carboxylesterase 3 esterase A, esterase B, esterase D, methylbutyrase, methylbutyrate ... has a role as a human carboxylesterase inhibitor. The carboxylesterase family of evolutionarily related proteins (those with ... The enzyme carboxylesterase (or carboxylic-ester hydrolase, EC 3.1.1.1; systematic name carboxylic-ester hydrolase) catalyzes ... Humans genes that encode carboxylesterase enzymes include: CES1 CES2 CES3 CES4 CES7 CES8 An approved nomenclature has been ...
Mouse Carboxylesterase 1 / CES1 protein (7929-CE) is manufactured by R&D Systems. Reproducible results in enzyme activity ... carboxylesterase 1 (monocyte/macrophage serine esterase 1); Carboxylesterase 1; carboxylesterase 2 (liver); CEH; CES1; Ces-1; ... Background: Carboxylesterase 1/CES1. Carboxylesterase 1 is a member of a large family of carboxylesterases that are responsible ... Reviews for Recombinant Mouse Carboxylesterase 1/CES1 Protein, CF. There are currently no reviews for this product. Be the ...
carboxylesterase 1. DDI. drug-drug interaction. [I]. inhibitor concentration. Imax maximal degree of inhibition. Imax, u ... In Vitro Inhibition of Carboxylesterase 1 by Major Cannabinoids and Selected Metabolites. Yuli Qian, Xinwen Wang and John S. ... Cannabinoid Inhibition of Carboxylesterase 1. Yuli Qian, Xinwen Wang and John S. Markowitz ... Cannabinoid Inhibition of Carboxylesterase 1. Yuli Qian, Xinwen Wang and John S. Markowitz ...
Six resistant carboxylesterase alleles (Ester) were recorded previously and sometimes co-existed in one field population, ... Correlation between carboxylesterase alleles and insecticide resistance in Culex pipiens complex from China. *Yangyang Liu1, ... Liu, Y., Zhang, H., Qiao, C. et al. Correlation between carboxylesterase alleles and insecticide resistance in Culex pipiens ... Six resistant carboxylesterase alleles (Ester) were recorded previously and sometimes co-existed in one field population, ...
enables carboxylesterase activity IDA Inferred from Direct Assay. more info. PubMed enables electron transfer activity TAS ...
Carboxylesterase 1D. Q8VCT4/NP_444430.2. Ces1d. 124. 2.7e-08. 33%. 15/31. 6.17/. 62,034. 1.12. 1.34. (*). 0.81. 1.20. 0.73. ... Liver specific inactivation of carboxylesterase 3/triacylglycerol hydrolase decreases blood lipids without causing severe ...
Comparison of the Structure and Activity of Glycosylated and Aglycosylated Human Carboxylesterase 1 ... Comparison of the Structure and Activity of Glycosylated and Aglycosylated Human Carboxylesterase 1 ...
Liver carboxylesterase 1. MWLRAFILATLSASAAWGHPSSPPVVDTVHGKVLGKFVSLEGFAQPVAIF.... unknown. Ferrochelatase. ...
Diketopyrrolopyrrole-based fluorescent probe for visualizing over-expressed carboxylesterase in fever via ratiometric imaging. ... including the important carboxylesterase (CE). Monitoring the activity changes of CE in vivo during a fever will help to ...
It was concluded that carboxylesterase in mouse plasma protects from high toxicity agents, but the amount of carboxylesterase ... It was concluded that carboxylesterase in mouse plasma protects from high toxicity agents, but the amount of carboxylesterase ... It was concluded that carboxylesterase in mouse plasma protects from high toxicity agents, but the amount of carboxylesterase ... It was concluded that carboxylesterase in mouse plasma protects from high toxicity agents, but the amount of carboxylesterase ...
Is genetic variability in carboxylesterase-1 and carboxylesterase-2 drug metabolism an important component of personalized ... Inhibition of carboxylesterase-1 alters clopidogrel metabolism and disposition. Xenobiotica 2019 DOI: 10.1080/00498254.2019. ... Does clopidogrel decrease the efficacy of carboxylesterase-1 prodrugs? Selected for presentation at the 2020 American Society ... Clinical implications of genetic variation in carboxylesterase metabolism. Expert Opin Drug Metab Toxicol 2018; 14:131-142. ...
Recombinant Human Lipase A GST (N-Term) Protein. Backed by our 100% Guarantee.
Name: carboxylesterase 2G. Synonyms: 2210023G05Rik. Type: Gene. Species: Mus musculus (mouse). Chromosome: 8 ...
carboxylesterase 1D. ISO. RGD. PMID:21621639. RGD:6484672. NCBI chr19:13,873,490...13,912,035 Ensembl chr19:13,796,623... ...
carboxylesterase 1D. multiple interactions. ISO. CES1 protein results in increased hydrolysis of and results in increased ...
Name: carboxylesterase 2H. Synonyms: Gm5744. Type: Gene. Species: Mus musculus (mouse). Chromosome: 8 ...
carboxylesterase activity. phospholipase a2 activity. Molecular Function. phospholipase A2 activity. calcium ion binding. ...
carboxylesterase 1. d-MPH. d-methylphenidate. dl-MPH. dl-methylphenidate. GC. gas chromatography. HFP. heptafluorobutyryl-S- ... 2008) Two CES1 gene mutations lead to dysfunctional carboxylesterase 1 activity in man: clinical significance and molecular ... 2010) Identification of selected therapeutic agents as inhibitors of carboxylesterase 1: potential sources of metabolic drug ... where circumvention of the oral hepatic first-pass effect-the organ that expresses carboxylesterase 1 (CES1), which catalyzes ...
Converted by the carboxylesterase enzyme to its active metabolite from, SN-38. SN-38 binds to and stabilizes the topoisomerase ...
lipid metabolism.lipid degradation.lysophospholipases.carboxylesterase. 1 (1.37%). 0. 0. 0. 0. 0. 0. 0. 0. 0. 0. 0. 0. 0. 0. 0 ...
CES1C (Carboxylesterase 1C (CES1C)) Binding Specificity AA 19-550 Reactivity All reactivities for CES1C antibodies * Mouse 13 ... anti-Carboxylesterase 1C (CES1C) (AA 19-550) antibody (FITC) CES1C Reactivity: Mouse ELISA, WB Host: Rabbit Polyclonal FITC ... anti-Carboxylesterase 1C (CES1C) (AA 19-550) antibody (HRP) CES1C Reactivity: Mouse ELISA Host: Rabbit Polyclonal HRP ... anti-Carboxylesterase 1C (CES1C) (AA 19-550) antibody (Biotin) CES1C Reactivity: Mouse, Rat ELISA, WB Host: Rabbit Polyclonal ...
With Tris-HCl buffer; human liver carboxylesterase pI 4.5 at 37℃; pH=7.4; Enzyme kinetics; Hydrolysis;. ...
A small portion is metabolized in the liver by carboxylesterase and less than 10% is metabolized by N -methylation in the liver ... In addition, alcohol allows carboxylesterase to transfer an ethyl group to cocaine to form cocaethylene. Cocaethylene, as is ...
Protein Families: Type-B carboxylesterase/lipase family. Tissue Specificity: Present in most cells except erythrocytes. ...
In the presence of alcohol, a nonspecific carboxylesterase catalyzes ethyl transesterification of cocaine to cocaethylene. ...
Carboxylesterase inhibition. *Carboxylesterase reaction phenotyping. *Aldehyde oxidase reaction phenotyping. Protein Binding. * ...
GO:0004091, F:carboxylesterase activity, IEA:UniProtKB-KW. GO:0046677, P:response to antibiotic, IEA:UniProtKB-KW. Family and ...
Protein Mammalian carboxylesterase (liver carboxylesterase I) [75282] (2 species). *. Species Human (Homo sapiens) [TaxId:9606] ... d1yaha1 c.69.1.1 (A:22-553) Mammalian carboxylesterase (liver carboxylesterase I) {Human (Homo sapiens) [TaxId: 9606]} ... PDB Description: crystal structure of human liver carboxylesterase complexed to etyl acetate; a fatty acid ethyl ester analogue ...
  • Humans genes that encode carboxylesterase enzymes include: CES1 CES2 CES3 CES4 CES7 CES8 An approved nomenclature has been established for the five mammalian carboxylesterase gene families. (wikipedia.org)
  • Although there have been a significant number of in vitro and in vivo assessments of the effects of cannabis on cytochrome P450 and UDP-glucuronosyltransferase enzyme systems, there is limited information regarding the effects of cannabis on the major hepatic esterase, carboxylesterase 1 (CES1). (aspetjournals.org)
  • However, simultaneous plasma monitoring of d-MPH and l-MPH may be warranted when alterations in first-pass hepatic metabolism by carboxylesterase 1 (CES1) occurs. (aspetjournals.org)
  • Irinotecan serves as a water-soluble precursor of the lipophilic metabolite SN-38, which is formed from irinotecan primarily by liver carboxylesterase enzymes. (rxmed.com)
  • The metabolic conversion of irinotecan to SN-38 is mediated by carboxylesterase enzymes primarily in the liver. (rxmed.com)
  • At 28d, serum acute phase proteins with immune function including complement C3, apolipoprotein A-I and A-II, alpha2-marcoglobulin, serotransferrin and liver carboxylesterase N were increased. (cdc.gov)
  • The enzyme carboxylesterase is omnipresent in the environment, readily degrading the test substances of this category. (europa.eu)
  • Biochemistry bioassays confirmed the involvement of monooxygenase enzyme, carboxylesterase, superoxide dismutase and peroxidase in multi-insecticide resistance mechanism. (preprints.org)
  • However, complete inhibition of carboxylesterase and butyrylcholinesterase has no known effect on an animal's well being. (nebraska.edu)
  • Inhibition of plasma acetylcholinesterase, butyrylcholinesterase, and plasma carboxylesterase was measured. (nebraska.edu)
  • Orthologous to human NOTUM (notum, palmitoleoyl-protein carboxylesterase). (zfin.org)
  • Diketopyrrolopyrrole-based fluorescent probe for visualizing over-expressed carboxylesterase in fever via ratiometric imaging. (bvsalud.org)
  • Mouse blood contains four esterases that detoxify organophosphorus compounds: carboxylesterase, butyrylcholinesterase, acetylcholinesterase, and paraoxonase-1. (nebraska.edu)
  • It was concluded that carboxylesterase in mouse plasma protects from high toxicity agents, but the amount of carboxylesterase in plasma is too low to protect from low toxicity compounds that require high doses to inhibit acetylcholinesterase. (nebraska.edu)
  • The carboxylesterase family of evolutionarily related proteins (those with clear sequence homology to each other) includes a number of proteins with different substrate specificities, such as acetylcholinesterases. (wikipedia.org)
  • Fever is the result of inflammation and the innate self -defense response of organisms, can cause abnormal changes in the activity of many enzymes in organisms, including the important carboxylesterase (CE). (bvsalud.org)
  • 20:4, n-6), formed by the synthesis from dietary linoleic acid (LA: C18H32O2 18:2, n-6), has a role as a human carboxylesterase inhibitor. (wikipedia.org)
  • In contrast human blood contains the latter three enzymes but not carboxylesterase. (nebraska.edu)
  • Carboxylesterase 1 is a member of a large family of carboxylesterases that are responsible for the hydrolysis of ester and amide bonds (1, 2). (rndsystems.com)
  • We have constructed a secreted form of human liver carboxylesterase-2 by deletion of the cellular retention signal and by cloning the cDNA downstream of an Ig kappa leader sequence. (johnshopkins.edu)
  • 2. Overexpression of a rabbit liver carboxylesterase sensitizes human tumor cells to CPT-11. (nih.gov)
  • 5. Sensitization of human tumor cells to CPT-11 via adenoviral-mediated delivery of a rabbit liver carboxylesterase. (nih.gov)
  • 7. Conversion of the CPT-11 metabolite APC to SN-38 by rabbit liver carboxylesterase. (nih.gov)
  • 8. Isolation and partial characterization of a cDNA encoding a rabbit liver carboxylesterase that activates the prodrug irinotecan (CPT-11). (nih.gov)
  • 13. Characterization of CPT-11 hydrolysis by human liver carboxylesterase isoforms hCE-1 and hCE-2. (nih.gov)
  • At 28d, serum acute phase proteins with immune function including complement C3, apolipoprotein A-I and A-II, alpha2-marcoglobulin, serotransferrin and liver carboxylesterase N were increased. (cdc.gov)
  • Organophosphate insecticide potentiation by carboxylesterase inhibitors. (cdc.gov)
  • Microsomal carboxylesterase activity in lung microsomes from 10 patients ranged from 19.02 ± 2.28 to 48.18 ± 4.34 nmol/mg protein/min, and was significantly decreased (25-45%) in microsomes incubated with phenylmethylsulfonyl fluoride, an inhibitor of the carboxylesterase enzyme. (aspetjournals.org)
  • This gene encodes a member of the type-B carboxylesterase/lipase protein family. (nih.gov)
  • Carboxylesterase is a serine-dependent esterase with wide substrate specificity. (nih.gov)
  • 15. Hydrolysis of irinotecan and its oxidative metabolites, 7-ethyl-10-[4-N-(5-aminopentanoic acid)-1-piperidino] carbonyloxycamptothecin and 7-ethyl-10-[4-(1-piperidino)-1-amino]-carbonyloxycamptothecin, by human carboxylesterases CES1A1, CES2, and a newly expressed carboxylesterase isoenzyme, CES3. (nih.gov)
  • 16. Proficient metabolism of irinotecan by a human intestinal carboxylesterase. (nih.gov)
  • 19. Mouse liver and kidney carboxylesterase (M-LK) rapidly hydrolyzes antitumor prodrug irinotecan and the N-terminal three quarter sequence determines substrate selectivity. (nih.gov)
  • 2-Naphthyl myristate is a substrate for carboxylesterase. (goldbio.com)
  • Converted by the carboxylesterase enzyme to its active metabolite from, SN-38. (medscape.com)
  • 20:4, n-6), formed by the synthesis from dietary linoleic acid (LA: C18H32O2 18:2, n-6), has a role as a human carboxylesterase inhibitor. (wikipedia.org)
  • An approach to achieve tumour specific activation of CPT-11 is to transduce the cDNA encoding carboxylesterase into tumour cells. (johnshopkins.edu)
  • To obtain a secreted, tumour-targeted form of carboxylesterase-2 the cDNA encoding the human scFv antibody C28 directed against the epithelial cell adhesion molecule EpCAM, was inserted between the leader sequence and carboxylesterase-2. (johnshopkins.edu)
  • 4. In vivo human carboxylesterase cDNA gene transfer to activate the prodrug CPT-11 for local treatment of solid tumors. (nih.gov)
  • Human carboxylesterase 2 (CES2) has triacylglycerol hydrolase (TGH) activities and plays an important role in lipolysis. (omeka.net)
  • Methylphenidate is stereoselectively hydrolyzed by human carboxylesterase CES1A1. (nih.gov)
  • Previous studies have shown that CYP2E1 and carboxylesterase enzymes contributed to vinyl carbamate (VC) metabolism in murine lung. (aspetjournals.org)
  • Here we have tested the hypothesis that CYP2E1 and carboxylesterase enzymes are involved also in VC metabolism in human lung. (aspetjournals.org)
  • 3. An improved human carboxylesterase for enzyme/prodrug therapy with CPT-11. (nih.gov)
  • 14. Enzyme-prodrug systems: carboxylesterase/CPT-11. (nih.gov)
  • 18. A virus-directed enzyme prodrug therapy approach to purging neuroblastoma cells from hematopoietic cells using adenovirus encoding rabbit carboxylesterase and CPT-11. (nih.gov)
  • Now known to be catalysed by EC 3.1.1.1 , carboxylesterase and EC 3.1.1.3 , triacylglycerol lipase. (genome.jp)
  • Carboxylesterase 1 gene polymorphism and methylphenidate response in ADHD. (cdc.gov)
  • Using this dosing regimen, we found that (1) the time of maximal ChE inhibition was the same (i.e., 5-10 h after dosing) for both maternal and fetal brain, (2) the degree of fetal brain ChE inhibition was 4.7 times less than maternal brain inhibition, and (3) the detoxification potential (i.e., carboxylesterase and chlorpyrifos-oxonase) of the fetal tissues was very low compared to the maternal tissues. (nih.gov)
  • The results showed that L. entomophila had significantly greater specific activity of carboxylesterase than L. bostrychophila (0.045 versus 0.012 µmoles /mg /min). (bioone.org)
  • CONCLUSION: A combination of in vitro biochemical assays and in vivo differential synergism studies using PBO and a close analogue EN 16/5-1 suggests that the mechanism conferring increased resistance in this clone is primarily due to enhanced oxidase activity. (rothamsted.ac.uk)
  • A secreted form of carboxylesterase may diffuse through a tumour mass and may activate CPT-11 extracellularly. (johnshopkins.edu)
  • 17. The role of rat serum carboxylesterase in the activation of paclitaxel and camptothecin prodrugs. (nih.gov)
  • In addition a secreted tumour-targeted form of carboxylesterase should prevent leakage of the enzyme from the site of the tumour into the circulation. (johnshopkins.edu)