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.
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.
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.
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.

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 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. Higher eukaryotes have many distinct esterases. 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 ...
K Moroi; T Kuga (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 ...
Hosokawa M, Satoh T (October 1993). "Differences in the induction of carboxylesterase isozymes in rat liver microsomes by ...
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 ...
August 2014). "Structural insights into the low pH adaptation of a unique carboxylesterase from Ferroplasma: altering the pH ...
Establishment and Characterization of a Novel Caco-2 Subclone with a Similar Low Expression Level of Human Carboxylesterase 1 ... Establishment and Characterization of a Novel Caco-2 Subclone with a Similar Low Expression Level of Human Carboxylesterase 1 ... Caco-2 cells predominantly express human carboxylesterase 1 (hCE1), unlike the human intestine that predominantly expresses ... human carboxylesterase 2 (hCE2). Transport experiments using Caco-2 cell monolayers often lead to misestimation of the ...
... carboxylesterase type B, block C, cholinesterases …) diverged from the other groups through simultaneous integration of an N- ... Within the alpha/beta hydrolase fold superfamily of proteins, the COesterase group (carboxylesterase type B, block C, ... An evolutionary perspective on the first disulfide bond in members of the cholinesterase-carboxylesterase (COesterase) family: ... An evolutionary perspective on the first disulfide bond in members of the cholinesterase-carboxylesterase (COesterase) family: ...
We found that the expression of carboxylesterase 1 (CES1) and cathepsin C (CTSC) was downregulated in HCM tissues and ... Weighted gene coexpression network analysis reveals negative regulation of hypertrophic cardiomyopathy by carboxylesterase 1 ...
Liver carboxylesterase 1. MWLRAFILATLSASAAWGHPSSPPVVDTVHGKVLGKFVSLEGFAQPVAIF.... unknown. substrate. UDP- ...
Murphy SD, Cheever KL, Chow AYK, Brewster M [1976]. Organophosphate insecticide potentiation by carboxylesterase inhibitors. ...
IPR002018 Carboxylesterase, type B. IPR019819 Carboxylesterase type B, conserved site. IPR000460 Neuroligin ...
carboxylesterase 1D. increases hydrolysis. EXP. CES1 protein results in increased hydrolysis of Palmitoyl Coenzyme A. CTD. PMID ...
DeCS 2008 - March 17, 2008 version. ...
Takaoka K., Ohtsuka K., Jin M. Conversion of CPT-11 to its active form SN-38, by carboxylesterase of non-small cell lung cancer ... Kojima A., Hackett N. R., Ohwada A., Crystal R. G. In vivo human carboxylesterase cDNA gene transfer to activate the prodrug ... Danks M. K., Morton C. L., Pawlik C. A., Potter P. M. Overexpression of a rabbit liver carboxylesterase sensitizes human tumor ... CPT-11 converting carboxylesterase and topoisomerase I activities in tumour and normal colon and liver tissues. Br. J. Cancer ...
Involvement of carboxylesterase-like proteins in leguminous isoflavone biosynthesis.. Journal. Plant Physiol 137:882-91 (2005) ...
Association of carboxylesterase B electrophoretic pattern with presence and expression of urovirulence factor determinants and ...
... in the promoter region of the flavone-inducible carboxylesterase gene CCE001j verified that the two motifs and ARE2 are not ...
Although some variability in the experimental results of carboxylesterase activity exists, depending on the methodology and the ... Although some variability in the experimental results of carboxylesterase activity exists, depending on the methodology and the ...
Carboxylesterase - Preferred Concept UI. M0090456. Scope note. Carboxylesterase is a serine-dependent esterase with wide ... 2004; CARBOXYLESTERASE was indexed under CARBOXYLIC ACID ESTERASES 1981-2003. History Note:. 2004; use CARBOXYLESTERASE (NM) ... Non specific Carboxylesterase Non specific Esterase Non-specific Carboxylesterase Non-specific Esterase Nonspecific Esterase ... Carboxylesterase B Carboxylesterase, Non-specific Carboxylic Ester Hydrolase Enzyme, CAP-hydrolyzing Enzyme, Capsaicin- ...
Immunoassay of carboxylesterase activity for identifying insecticide resistant Myzus persicae. Proceedings of the British Crop ... Carboxylesterase FE4 - green peach aphid (564 residues). K - Protein or DNA sequences submitted to database ... Carboxylesterase E4 - green peach aphid (552 residues). K - Protein or DNA sequences submitted to database ... Immunoassay of carboxylesterase activity for identifying insecticide resistant Myzus persicae. A - Papers appearing in refereed ...
... catalase and carboxylesterase activities have been evaluated in liver of Cyprinus carpio. The level of OCPs were determined by ...
https://doi.org/10.18632/oncotarget.20719 Meng Rao, Sha Ma, Shifu Hu, Hui Lei, Yanqing Wu, Yanfei Zhou, Wei Xia, Changhong Zhu
F:carboxylesterase activity;P:biological_process unknown;C:unknown;PMOB. O.I.. C.G.. H.G.. Please select. TAIR (integral). KEGG ...
Carboxylesterase. 9bila-a0a0d6mab5. Arylacetamide_deacetylase. Ancylostoma ceylanicum. Hydrolase, alpha/beta domain protein. ...
... the carboxylesterase (CE; PF00135; n = 152) domain was found in a large number of transcripts. The CEs are general ...
Carboxylesterase family. PRK10162. PRK10162. 3.0e-11. 81. 224. 144. + acetyl esterase; Provisional ...
LYsophospholipase_carboxylesterase : xanax-XAC0619Xanthomonas axonopodis (pv. citri) Xanthomonas campestris pv. vesicatoria ... aurantifolii carboxylesterase.. Monoglyceridelipase_lysophospholip : xanax-XAC0515Xanthomonas axonopodis, Xanthomonas ... carboxylesterase, xanax-XAC3315Xanthomonas axonopodis, Xanthomonas fuscans, Xanthomonas vesicatoria, Xanthomonas perforans, ...
carboxylesterase (RefSeq). 29, 149. BSU35190. yvkC. putative phosphotransferase (RefSeq). 180, 248. BSU35970. ywsB. ...
Phospholipase/Carboxylesterase. 5.2E-06. 5. 207. GO. GO Term. Description. Terminal node. ...
Expression and characterization of the carboxyl esterase Rv3487c from Mycobacterium tuberculosis. Protein Expr Purif. 2005;42(1 ... This gene encodes for a lipase with phospholipase C and carboxylesterase activities and has particularly high activity with ...
  • From NCBI Gene: This gene encodes a cholinesterase enzyme and member of the type-B carboxylesterase/lipase family of proteins. (nih.gov)
  • Within the alpha/beta hydrolase fold superfamily of proteins, the COesterase group (carboxylesterase type B, block C, cholinesterases …) diverged from the other groups through simultaneous integration of an N-terminal, first disulfide bond and a significant increase in the protein mean size. (inrae.fr)
  • Caco-2 cells predominantly express human carboxylesterase 1 (hCE1), unlike the human intestine that predominantly expresses human carboxylesterase 2 (hCE2). (aspetjournals.org)
  • 3. An improved human carboxylesterase for enzyme/prodrug therapy with CPT-11. (nih.gov)
  • 4. In vivo human carboxylesterase cDNA gene transfer to activate the prodrug CPT-11 for local treatment of solid tumors. (nih.gov)
  • 9. Secreted and tumour targeted human carboxylesterase for activation of irinotecan. (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)
  • Because of high levels in the urine of male domestic cats, this enzyme is also called cauxin (carboxylesterase-like urinary excreted protein). (nih.gov)
  • Involvement of carboxylesterase-like proteins in leguminous isoflavone biosynthesis. (genome.jp)
  • 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)
  • We found that the expression of carboxylesterase 1 (CES1) and cathepsin C (CTSC) was downregulated in HCM tissues and negatively correlated with Maxi LVWT. (bvsalud.org)
  • Irinotecan itself is a prodrug that must be activated to SN-38 by carboxylesterase. (medscape.com)
  • 8. Isolation and partial characterization of a cDNA encoding a rabbit liver carboxylesterase that activates the prodrug irinotecan (CPT-11). (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. 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)
  • 13. Characterization of CPT-11 hydrolysis by human liver carboxylesterase isoforms hCE-1 and hCE-2. (nih.gov)
  • Ethoxyresorufin O-deethylase, glutathion Stransferase, glutathion reductase, superoxide dismutase, catalase and carboxylesterase activities have been evaluated in liver of Cyprinus carpio. (trjfas.org)
  • Irinotecan is primarily metabolized by carboxylesterase to the active metabolite, SN-38, which is responsible for inhibition of DNA topoisomerase I. SN-38 is glucuronidated by UGT1A1 to the inactive metabolite SN-38G, which is subsequently excreted. (medscape.com)
  • Other irinotecan inactivation pathways include oxidation by CYP3A4 and CYP3A5 into APC and NPC, which can also be metabolized by carboxylesterase to SN-38. (medscape.com)
  • 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)
  • Weighted gene coexpression network analysis reveals negative regulation of hypertrophic cardiomyopathy by carboxylesterase 1 and cathepsin C. (bvsalud.org)
  • This gene encodes a member of the carboxylesterase large family. (nih.gov)
  • 17. The role of rat serum carboxylesterase in the activation of paclitaxel and camptothecin prodrugs. (nih.gov)
  • Carboxylesterase is a serine-dependent esterase with wide substrate specificity. (nih.gov)
  • Although some variability in the experimental results of carboxylesterase activity exists, depending on the methodology and the substrate used, there is a general trend supporting lower nasal esterase activity towards esters from human tissues compared to those from rat tissues. (europa.eu)
  • 1. Overexpression of a rabbit liver carboxylesterase sensitizes human tumor cells to CPT-11. (nih.gov)
  • 3. Conversion of the CPT-11 metabolite APC to SN-38 by rabbit liver carboxylesterase. (nih.gov)
  • 4. Isolation and partial characterization of a cDNA encoding a rabbit liver carboxylesterase that activates the prodrug irinotecan (CPT-11). (nih.gov)
  • 5. Sensitization of human tumor cells to CPT-11 via adenoviral-mediated delivery of a rabbit liver carboxylesterase. (nih.gov)
  • 16. Characterization of CPT-11 hydrolysis by human liver carboxylesterase isoforms hCE-1 and hCE-2. (nih.gov)
  • 18. p53-mediated regulation of expression of a rabbit liver carboxylesterase confers sensitivity to 7-ethyl-10-[4-(1-piperidino)-1-piperidino]carbonyloxycamptothecin (CPT-11). (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)
  • 7. Proficient metabolism of irinotecan by a human intestinal carboxylesterase. (nih.gov)
  • 8. 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)
  • 13. Secreted and tumour targeted human carboxylesterase for activation of irinotecan. (nih.gov)