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[PMID]:27062891
[Au] Autor:Lozano-Paniagua D; Gómez-Martín A; Gil F; Parrón T; Alarcón R; Requena M; Lacasaña M; Hernández AF
[Ad] Endereço:Dept. Legal Medicine and Toxicology, University of Granada School of Medicine, Spain.
[Ti] Título:Activity and determinants of cholinesterases and paraoxonase-1 in blood of workers exposed to non-cholinesterase inhibiting pesticides.
[So] Source:Chem Biol Interact;259(Pt B):160-167, 2016 Nov 25.
[Is] ISSN:1872-7786
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Pesticide exposure has been associated with different adverse health effects which may be modulated to some extent by paraoxonase-1 (PON1) activity and genetic polymorphisms. This study assessed seasonal variations in PON1 activity (using paraoxon -POase-, phenylacetate -AREase-, diazoxon -DZOase- and dihydrocoumarin -DHCase- as substrates), erythrocyte acetylcholinesterase (AChE) and plasma cholinesterase (using butyrylthiocholine -BuChE- and benzoylcholine -BeChE- as substrates. The study population consisted of intensive agriculture workers regularly exposed to pesticides other than organophosphates and non-exposed controls from Almería (Southeastern Spain). The effect of common genetic polymorphisms of PON1 and BCHE on paraoxonase-1 and cholinesterase activities toward different substrates was also assessed. Linear mixed models were used to compare esterase activities in agricultural workers and control subjects over the two study periods (high and low exposure to pesticides). The significant decrease in AChE and increase in BuChE and BeChE activities observed in workers with respect to control subjects was attributed to pesticide exposure. Workers also had higher levels of AREase, DZOase and, to a lesser extent, of POase, but showed decreased DHCase activity. While PON1 Q192R and PON1 -108C/T gene polymorphisms were significantly associated with all PON1 activities, PON1 L55M showed a significant association with AREase, DZOase and DHCase. BCHE-K (Karlow variant) was significantly associated with lower BeChE activity (but not with BuChE) and BCHE-A (atypical variant) showed no significant association with any cholinesterase activity. These findings suggest that increased PON1, BuChE and BeChE activities in exposed workers might result from an adaptive response against pesticide exposure to compensate for adverse effects at the biochemical level. This response appears to be modulated by PON1 and BCHE gene polymorphisms.
[Mh] Termos MeSH primário: Acetilcolinesterase/metabolismo
Arildialquilfosfatase/metabolismo
Praguicidas/envenenamento
[Mh] Termos MeSH secundário: Acetilcolinesterase/sangue
Adolescente
Adulto
Idoso
Arildialquilfosfatase/genética
Benzoilcolina/química
Benzoilcolina/metabolismo
Butiriltiocolina/química
Butiriltiocolina/metabolismo
Eritrócitos/enzimologia
Eritrócitos/metabolismo
Feminino
Genótipo
Seres Humanos
Estudos Longitudinais
Masculino
Meia-Idade
Polimorfismo de Nucleotídeo Único
Reação em Cadeia da Polimerase em Tempo Real
Especificidade por Substrato
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pesticides); 2208-04-0 (Benzoylcholine); 4555-00-4 (Butyrylthiocholine); EC 3.1.1.7 (Acetylcholinesterase); EC 3.1.8.1 (Aryldialkylphosphatase); EC 3.1.8.1 (PON1 protein, human)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170201
[Lr] Data última revisão:
170201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160412
[St] Status:MEDLINE


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[PMID]:24254312
[Au] Autor:Bussell JD; Reichelt M; Wiszniewski AA; Gershenzon J; Smith SM
[Ad] Endereço:Australian Research Council Centre of Excellence in Plant Energy Biology, University of Western Australia, Crawley, Western Australia 6009, Australia.
[Ti] Título:Peroxisomal ATP-binding cassette transporter COMATOSE and the multifunctional protein abnormal INFLORESCENCE MERISTEM are required for the production of benzoylated metabolites in Arabidopsis seeds.
[So] Source:Plant Physiol;164(1):48-54, 2014 Jan.
[Is] ISSN:1532-2548
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Secondary metabolites derived from benzoic acid (BA) are of central importance in the interactions of plants with pests, pathogens, and symbionts and are potentially important in plant development. Peroxisomal ß-oxidation has recently been shown to contribute to BA biosynthesis in plants, but not all of the enzymes involved have been defined. In this report, we demonstrate that the peroxisomal ATP-binding cassette transporter COMATOSE is required for the accumulation of benzoylated secondary metabolites in Arabidopsis (Arabidopsis thaliana) seeds, including benzoylated glucosinolates and substituted hydroxybenzoylcholines. The ABNORMAL INFLORESCENCE MERISTEM protein, one of two multifunctional proteins encoded by Arabidopsis, is essential for the accumulation of these compounds, and MULTIFUNCTIONAL PROTEIN2 contributes to the synthesis of substituted hydroxybenzoylcholines. Of the two major 3-ketoacyl coenzyme A thiolases, KAT2 plays the primary role in BA synthesis. Thus, BA biosynthesis in Arabidopsis employs the same core set of ß-oxidation enzymes as in the synthesis of indole-3-acetic acid from indole-3-butyric acid.
[Mh] Termos MeSH primário: Transportadores de Cassetes de Ligação de ATP/metabolismo
Proteínas de Arabidopsis/metabolismo
Arabidopsis/metabolismo
Ácido Benzoico/metabolismo
Complexos Multienzimáticos/metabolismo
Sementes/metabolismo
[Mh] Termos MeSH secundário: Transportadores de Cassetes de Ligação de ATP/genética
Arabidopsis/genética
Proteínas de Arabidopsis/genética
Benzoilcolina/análogos & derivados
Benzoilcolina/química
Benzoilcolina/metabolismo
Colina/química
Colina/metabolismo
Cinamatos/metabolismo
Regulação da Expressão Gênica de Plantas
Glucosinolatos/metabolismo
Complexos Multienzimáticos/genética
Mutação
Oxirredução
Canais de Potássio de Abertura Dependente da Tensão da Membrana/genética
Canais de Potássio de Abertura Dependente da Tensão da Membrana/metabolismo
Ácido Salicílico/metabolismo
Metabolismo Secundário
Sementes/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (AIM1 protein, Arabidopsis); 0 (Arabidopsis Proteins); 0 (Cinnamates); 0 (Glucosinolates); 0 (KAT2 protein, Arabidopsis); 0 (Multienzyme Complexes); 0 (Ped3 protein, Arabidopsis); 0 (Potassium Channels, Voltage-Gated); 2208-04-0 (Benzoylcholine); 5094-31-5 (4-hydroxybenzoylcholine); 8SKN0B0MIM (Benzoic Acid); N91BDP6H0X (Choline); O414PZ4LPZ (Salicylic Acid); U14A832J8D (cinnamic acid)
[Em] Mês de entrada:1410
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131121
[St] Status:MEDLINE
[do] DOI:10.1104/pp.113.229807


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[PMID]:22762247
[Au] Autor:Lee S; Kaminaga Y; Cooper B; Pichersky E; Dudareva N; Chapple C
[Ad] Endereço:Department of Biochemistry, Purdue University, West Lafayette, IN 47907, USA.
[Ti] Título:Benzoylation and sinapoylation of glucosinolate R-groups in Arabidopsis.
[So] Source:Plant J;72(3):411-22, 2012 Nov.
[Is] ISSN:1365-313X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Glucosinolates (GSLs) are nitrogen- and sulfur-containing metabolites that contribute to human health and plant defense. The biological activities of these molecules are largely dependent on modification of the GSL R-groups derived from their corresponding amino acid precursors. In Arabidopsis seeds, esterification of the R-group of hydroxylated GSLs (OH-GSLs) leads to the accumulation of benzoylated GSLs (BzGSLs) and sinapoylated GSLs (SnGSLs). BzGSLs were thought to be synthesized from OH-GSLs and benzoyl CoA by a BAHD acyltransferase, but no BAHD gene is strongly co-expressed with the two reference genes BZO1 and AOP3 that are required for BzGSL biosynthesis. In contrast, three genes encoding serine carboxypeptidase-like (SCPL) acyltransferases [SCPL5, SCPL17 and SCPL19 (SNG2)] do exhibit strong co-expression. Using a reverse genetic approach, we found that the GSL profile of the scpl5 mutant was identical to that of wild-type, but both BzGSLs and SnGSLs were barely detectable in scpl17 mutants and their amounts were decreased in the sng2 mutant. In addition, both scpl17 and sng2 mutants accumulate the putative BzGSL precursors OH-GSLs and benzoylglucose. The results of further GSL analyses in other phenylpropanoid mutants and benzoate feeding experiments suggested that SCPL17 mediates the acyltransferase reaction directly, while the mutation in sng2 causes a decrease in BzGSLs and SnGSLs via an unknown indirect mechanism. Finally, benzoate feeding experiments using bzo1 mutants and BZO1 biochemical characterization indicated that the in vivo role of BZO1 is to synthesize the benzoate precursor cinnamoyl CoA rather than to generate benzoyl CoA from benzoate and CoA as previously predicted.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/enzimologia
Benzoatos/metabolismo
Ácidos Cumáricos/metabolismo
Glucosinolatos/metabolismo
[Mh] Termos MeSH secundário: Acil Coenzima A/metabolismo
Aciltransferases/genética
Aciltransferases/metabolismo
Arabidopsis/efeitos dos fármacos
Arabidopsis/genética
Arabidopsis/metabolismo
Proteínas de Arabidopsis/genética
Benzoatos/química
Benzoatos/farmacologia
Benzoilcolina/química
Benzoilcolina/metabolismo
Vias Biossintéticas
Carboxipeptidases
Cinamatos/química
Cinamatos/metabolismo
Coenzima A Ligases/genética
Coenzima A Ligases/metabolismo
Ácidos Cumáricos/química
Esterificação
Teste de Complementação Genética
Glucosídeos/química
Glucosídeos/metabolismo
Glucosinolatos/análise
Glucosinolatos/química
Cinética
Mutação
Fenótipo
Propanóis/química
Propanóis/metabolismo
Sementes/genética
Sementes/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Arabidopsis Proteins); 0 (Benzoates); 0 (Cinnamates); 0 (Coumaric Acids); 0 (Glucosides); 0 (Glucosinolates); 0 (Propanols); 0 (sinapoylglucose); 0F897O3O4M (1-phenylpropanol); 2208-04-0 (Benzoylcholine); 68A28V6010 (sinapinic acid); 76109-04-1 (cinnamoyl-coenzyme A); EC 2.3.- (Acyltransferases); EC 3.4.- (Carboxypeptidases); EC 3.4.16.5 (serine carboxypeptidase); EC 6.2.1.- (Coenzyme A Ligases); EC 6.2.1.25 (BZO1 protein, Arabidopsis)
[Em] Mês de entrada:1304
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120706
[St] Status:MEDLINE
[do] DOI:10.1111/j.1365-313X.2012.05096.x


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[PMID]:22570941
[Au] Autor:Sisková K; Bilka F; Adameová A; Balazová A; Mydla M; Pauliková I
[Ad] Endereço:Department of Cell and Molecular Biology of Drugs, Faculty of Pharmacy, Comenius University, Bratislava, Slovak Republic. katarina.siskova@gmail.com
[Ti] Título:Influence of lipid imbalance on butyrylcholinesterase activity and biotransformation efficiency.
[So] Source:Pharmazie;67(4):345-50, 2012 Apr.
[Is] ISSN:0031-7144
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Butyrylcholinesterase (EC 3.1.1.8, BChE) is highly active in plasma, skin and lung, the tissues that first contact xenobiotics, supporting a role for BChE in detoxication of xenobiotics including medicaments. A possible involvement of BChE in lipid metabolism has been suggested. Elevated BChE activity in obese individuals correlates with some parameters of lipid metabolism including increased levels of triacylglycerols (TAG) and cholesterol. The aim of this study was to estimate the BChE activity in rats on subcellular and inter-organ levels under the conditions of untreated and treated primary hypertriacylglycerolemia with the TAG lowering agent fenofibrate. No changes in BChE activity were observed in obese animals. However fenofibrate administration led to significant increase of BChE activity in all examined tissues (plasma, liver, white adipose tissue). The impact of lipid metabolic imbalance on BChE biotransformation ability was tested by measuring the rate of hydrolysis of 0,1 to 8 mM concentrations of the antimicrobial agent N-(2-benzoyloxyethyl)-ethyldimethylammonium bromide (BCH2). The results revealed a complete shift in the BChE kinetics in all studied models. In animals with hypertriacylglycerolemia the Km value of liver BChE rised 4,6-fold, but the total enzyme efficiency expressed as Vmax/Km dropped 40% comparing to control. In contrast, in animals treated with fenofibrate the BChE efficiency increased in liver 1,6-fold. We conclude here that BChE detoxification capacity is essentially altered under conditions of disturbed lipid metabolism. Clinically, this knowledge could be important in a view of xenobiotic elimination, especially when routinely prescribed medicaments are concerned.
[Mh] Termos MeSH primário: Butirilcolinesterase/metabolismo
Transtornos do Metabolismo dos Lipídeos/metabolismo
[Mh] Termos MeSH secundário: Tecido Adiposo Branco/metabolismo
Animais
Benzoilcolina/metabolismo
Biotransformação
Peso Corporal/fisiologia
Butirilcolinesterase/sangue
Cromatografia Líquida de Alta Pressão
Citosol/metabolismo
Dieta
Fenofibrato/farmacologia
Hiperlipidemias/metabolismo
Hipolipemiantes/farmacologia
Transtornos do Metabolismo dos Lipídeos/sangue
Fígado/metabolismo
Masculino
Microssomos Hepáticos/metabolismo
RNA/biossíntese
RNA/isolamento & purificação
Ratos
Ratos Wistar
Reação em Cadeia da Polimerase em Tempo Real
Triglicerídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hypolipidemic Agents); 0 (Triglycerides); 2208-04-0 (Benzoylcholine); 63231-63-0 (RNA); EC 3.1.1.8 (Butyrylcholinesterase); U202363UOS (Fenofibrate)
[Em] Mês de entrada:1206
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120511
[St] Status:MEDLINE


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[PMID]:19618678
[Au] Autor:Pauliková I; Sisková K
[Ad] Endereço:Department of Cell and Molecular Biology of Drugs, Faculty of Pharmacy, Comenius University, Kalinciakova 8, 832 32 Bratislava, Slovakia. paulikova@fpharm.uniba.sk
[Ti] Título:Enzymes cooperating in the hydrolyzing process of benzoylcholines: subcellular and inter-tissue comparison.
[So] Source:Pharmazie;64(6):398-402, 2009 Jun.
[Is] ISSN:0031-7144
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Within benzoylcholine biotransformation, butyrylcholinesterase (3.1.1.8, BuChE) appears to be the key enzyme in the hydrolyzing process. Except for BuChE in the process of benzoylcholine hydrolysis, carboxylesterase (3.1.1.1, CE) could play a role in the splitting of the ester bond. The aim of this work was to clarify the interaction between BuChE and CE in the hydrolyzing process of a homologic row of benzolycholines on subcellular and inter-tissue level. Two fractions, microsomes and cytosol of rabbit lung and liver were investigated. Participation of the enzyme activities was determined on the base of kinetic inhibitory studies, using eserine as cholinesterase inhibitor. Despite the fact that in all studied fractions of both organs BuChE and CE were confirmed, only in lung microsomes exclusive BuChE activity in benzoylcholine hydrolyzing process was observed, without substrate specifity. In the other fractions studied interaction of both enzymes were recorded, whereas the benzoylcholine structure played an important role. It seems that, the portion of CE depends predominantly on substrate structure and elevates with bulk of alcoholic part of benzoylcholines. Despite the same enzyme equipment in all tissue fractions studied, the affinity of hydrolyzing enzymes interestingly differs. This might be as a result of distinct subcellular pattern of CE activity localization in lung and liver.
[Mh] Termos MeSH primário: Benzoilcolina/metabolismo
Butirilcolinesterase/metabolismo
Carboxilesterase/metabolismo
Fígado/enzimologia
Pulmão/enzimologia
Frações Subcelulares/enzimologia
[Mh] Termos MeSH secundário: Animais
Cromatografia Líquida de Alta Pressão
Citosol/enzimologia
Hidrólise
Técnicas In Vitro
Cinética
Masculino
Microssomos/enzimologia
Microssomos Hepáticos/enzimologia
Especificidade de Órgãos
Coelhos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
2208-04-0 (Benzoylcholine); EC 3.1.1.1 (Carboxylesterase); EC 3.1.1.8 (Butyrylcholinesterase)
[Em] Mês de entrada:0909
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090722
[St] Status:MEDLINE


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[PMID]:18620919
[Au] Autor:Hsieh BC; Hsiao HY; Cheng TJ; Chen RL
[Ad] Endereço:Department of Bio-Industrial Mechatronics Engineering, National Taiwan University, 136 Chou-Shan Road, Taipei City 106, Taiwan, ROC.
[Ti] Título:Assays for serum cholinesterase activity by capillary electrophoresis and an amperometric flow injection choline biosensor.
[So] Source:Anal Chim Acta;623(2):157-62, 2008 Aug 15.
[Is] ISSN:1873-4324
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:A capillary electrophoresis method and a durable choline biosensor were developed for measuring serum cholinesterase (EC 3.1.1.8) activity, a useful clinical index for liver function. The former is based on separation of benzoate and benzoylcholine (the artificial substrate of cholinesterase) in an uncoated fused-silica capillary. The migration time of benzoylcholine and benzoate was 1.3 min and 5.5 min, respectively. By the peak areas of A(233) signals, the linear dynamic ranges for both analytes were 0.01-50.0 mM, and the relative standard deviations of 1.0 mM benzoylcholine and benzoate were less than 4% and 6%, respectively. The FIA-choline sensor was constructed with the working electrode of the flow cell covered with a natural chitinous membrane purified from Taiwanese soldier crab, Mictyris brevidactylus. The biomembrane served as the supporting material for enzyme immobilization (choline oxidase, EC 1.1.3.17), and also prevented protein adsorption on the electrode surface. The calibration curve was linear between 0.05 and 5.0 mM (r=0.999). The relative standard deviations for 1.0 mM choline (n=7) were less than 3%, and the activity of the bioactive membrane lasted for about 2 months. The analytical results of both methods correlated well (r=0.940).
[Mh] Termos MeSH primário: Técnicas Biossensoriais/instrumentação
Colina/metabolismo
Colinesterases/sangue
Eletroforese Capilar/métodos
Análise de Injeção de Fluxo/métodos
[Mh] Termos MeSH secundário: Animais
Benzoatos/isolamento & purificação
Benzoatos/metabolismo
Benzoilcolina/isolamento & purificação
Benzoilcolina/metabolismo
Quitina/química
Colinesterases/metabolismo
Eletroquímica
Seres Humanos
Concentração de Íons de Hidrogênio
Membranas Artificiais
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzoates); 0 (Membranes, Artificial); 1398-61-4 (Chitin); 2208-04-0 (Benzoylcholine); EC 3.1.1.8 (Cholinesterases); N91BDP6H0X (Choline)
[Em] Mês de entrada:0810
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:080716
[St] Status:MEDLINE
[do] DOI:10.1016/j.aca.2008.06.008


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[PMID]:17531543
[Au] Autor:Mohamed MA; Abdel-Gawad AS; Ghazy AE
[Ad] Endereço:Molecular Biology Department, National Research Centre, Cairo, Egypt. magdasoroor@yahoo.com
[Ti] Título:Purification and characterization of an acetylcholinesterase from the infective juveniles of Heterorhabditis bacteriophora.
[So] Source:Comp Biochem Physiol C Toxicol Pharmacol;146(3):314-24, 2007 Sep.
[Is] ISSN:1532-0456
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acetylcholinesterases (AChEs) have been estimated in the infective juveniles (IJs) of eight different strains of heterorhabditid nematodes. The enzyme content ranged from 45.6 to 421.3 units/10(5) IJs with specific activity 34.0 to 82.6 units/mg protein. The isoenzyme patterns revealed the existence of two-slow-moving isoforms. Heterorhabditis bacteriophora AChE1A has been purified from the IJs of the heterorhabditid nematode strain of the highest enzymatic activity to homogeneity by ammonium sulfate precipitation, gel filtration on Sephacryl S-200 and DEAE-Sepharose. The specific activity of the purified enzyme was 1378.1 units/mg protein with purification fold 17.5 over crude extract. The enzyme has a pH optimum at 7.5. The optimum temperature for enzyme activity and stability was 35 degrees C. The activation energy was calculated to be 9.0 kcal/mol. The enzyme hydrolyzes acetylthiocholine (AcSCh), propionylthiocholine (PrSCh), S-butyrylthiocholine (BuSCh) and benzoylthiocholine (BzSCh) iodides with relative rate 100, 74.6, 41.7 and 22.2%, respectively. It displayed an apparent Michaelis-Menten behavior in the concentration range from 0.1 to 2 mM for the three former substrates with Km values 0.27, 0.42 and 0.59 mM, respectively. H. bacteriophora ChE1A is an AChE since it hydrolyzed AcSChI at higher rate than the other substrates and displayed excess substrate inhibition with AcSChI at concentrations over 2 mM. It was inhibited by eserine and BW284C51, but not by iso-OMPA. Its biochemical properties were compared with those reported for different species of insects as target hosts for heterorhabditid nematodes and animal parasitic nematodes.
[Mh] Termos MeSH primário: Acetilcolinesterase/isolamento & purificação
Acetilcolinesterase/metabolismo
Estágios do Ciclo de Vida/fisiologia
Rhabditoidea/enzimologia
[Mh] Termos MeSH secundário: Acetiltiocolina/metabolismo
Animais
Benzoilcolina/análogos & derivados
Benzoilcolina/metabolismo
Butiriltiocolina/metabolismo
Hidrólise
Especificidade por Substrato
Tiocolina/análogos & derivados
Tiocolina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (benzoylthiocholine); 2208-04-0 (Benzoylcholine); 24578-90-3 (propionylthiocholine); 4468-05-7 (Acetylthiocholine); 4555-00-4 (Butyrylthiocholine); 625-00-3 (Thiocholine); EC 3.1.1.7 (Acetylcholinesterase)
[Em] Mês de entrada:0710
[Cu] Atualização por classe:070806
[Lr] Data última revisão:
070806
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:070529
[St] Status:MEDLINE


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[PMID]:17182295
[Au] Autor:Masson P; Froment MT; Gillon E; Nachon F; Lockridge O; Schopfer LM
[Ad] Endereço:Centre de Recherches du Service de Santé des Armées, Unité d'Enzymologie, BP 87, 38702 La Tronche Cedex, France. pmasson@unmc.edu
[Ti] Título:Hydrolysis of oxo- and thio-esters by human butyrylcholinesterase.
[So] Source:Biochim Biophys Acta;1774(1):16-34, 2007 Jan.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Catalytic parameters of human butyrylcholinesterase (BuChE) for hydrolysis of homologous pairs of oxo-esters and thio-esters were compared. Substrates were positively charged (benzoylcholine versus benzoylthiocholine) and neutral (phenylacetate versus phenylthioacetate). In addition to wild-type BuChE, enzymes containing mutations were used. Single mutants at positions: G117, a key residue in the oxyanion hole, and D70, the main component of the peripheral anionic site were tested. Double mutants containing G117H and mutations on residues of the oxyanion hole (G115, A199), or the pi-cation binding site (W82), or residue E197 that is involved in stabilization of tetrahedral intermediates were also studied. A mathematical analysis was used to compare data for BuChE-catalyzed hydrolysis of various pairs of oxo-esters and thio-esters and to determine the rate-limiting step of catalysis for each substrate. The interest and limitation of this method is discussed. Molecular docking was used to analyze how the mutations could have altered the binding of the oxo-ester or the thio-ester. Results indicate that substitution of the ethereal oxygen for sulfur in substrates may alter the adjustment of substrate in the active site and stabilization of the transition-state for acylation. This affects the k2/k3 ratio and, in turn, controls the rate-limiting step of the hydrolytic reaction. Stabilization of the transition state is modulated both by the alcohol and acyl moieties of substrate. Interaction of these groups with the ethereal hetero-atom can have a neutral, an additive or an antagonistic effect on transition state stabilization, depending on their molecular structure, size and enantiomeric configuration.
[Mh] Termos MeSH primário: Butirilcolinesterase/metabolismo
[Mh] Termos MeSH secundário: Acilação
Substituição de Aminoácidos
Benzoilcolina/análogos & derivados
Benzoilcolina/metabolismo
Butirilcolinesterase/genética
Glicolatos/metabolismo
Seres Humanos
Hidrólise
Cinética
Organofosfatos/metabolismo
Fenilacetatos/metabolismo
Relação Estrutura-Atividade
Especificidade por Substrato
Tiocolina/análogos & derivados
Tiocolina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Glycolates); 0 (Organophosphates); 0 (Phenylacetates); 0 (benzoylthiocholine); 2208-04-0 (Benzoylcholine); 625-00-3 (Thiocholine); EC 3.1.1.8 (Butyrylcholinesterase); ER5I1W795A (phenylacetic acid); M12342PPGS (thiophenoxyacetic acid)
[Em] Mês de entrada:0703
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:061222
[St] Status:MEDLINE


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[PMID]:16519684
[Au] Autor:Hrabovská A; Debouzy JC; Froment MT; Devínsky F; Pauliková I; Masson P
[Ad] Endereço:Comenius University, Faculty of Pharmacy, Department of Cell and Molecular Biology of Drugs, Bratislava, Slovakia. hrabovska@pharm.uniba.sk
[Ti] Título:Rat butyrylcholinesterase-catalysed hydrolysis of N-alkyl homologues of benzoylcholine.
[So] Source:FEBS J;273(6):1185-97, 2006 Mar.
[Is] ISSN:1742-464X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The purpose of this work was to study the catalytic properties of rat butyrylcholinesterase with benzoylcholine (BzCh) and N-alkyl derivatives of BzCh (BCHn) as substrates. Complex hysteretic behaviour was observed in the approach to steady-state kinetics for each ester. Hysteresis consisted of a long lag phase with damped oscillation. The presence of a long lag phase, with no oscillations, in substrate hydrolysis by rat butyrylcholinesterase was also observed with N-methylindoxyl acetate as substrate. Hysteretic behaviour was explained by the existence of two interconvertible butyrylcholinesterase forms in slow equilibrium, while just one of them is catalytically active. The damped oscillations were explained by the existence of different substrate conformational states and/or aggregates (micelles) in slow equilibrium. Different substrate conformational states were confirmed by 1H-NMR. The K(m) values for substrates decreased as the length of the alkyl chain increased. High affinity of the enzyme for the longest alkyl chain length substrates was explained by multiple hydrophobic interactions of the alkyl chain with amino acid residues lining the active site gorge. Molecular modelling studies supported this interpretation; docking energy decreased as the length of the alkyl chain increased. The long-chain substrates had reduced k(cat) values. Docking studies showed that long-chain substrates were not optimally oriented in the active site for catalysis, thus explaining the slow rate of hydrolysis. The hydrolytic rate of BCH12 and longer alkyl chain esters vs. substrate concentration showed a premature plateau far below V(max). This was due to the loss of substrate availability. The best substrates for rat butyrylcholinesterase were short alkyl homologues, BzCh - BCH4.
[Mh] Termos MeSH primário: Benzoilcolina/metabolismo
Butirilcolinesterase/química
Butirilcolinesterase/metabolismo
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação
Catálise
Colinesterases/metabolismo
Hidrólise
Cinética
Modelos Moleculares
Estrutura Molecular
Oscilometria
Ligação Proteica
Conformação Proteica
Ratos
Estereoisomerismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
2208-04-0 (Benzoylcholine); EC 3.1.1.8 (Butyrylcholinesterase); EC 3.1.1.8 (Cholinesterases)
[Em] Mês de entrada:0605
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:060308
[St] Status:MEDLINE


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[PMID]:16434764
[Au] Autor:Wiesner G; Hartwig M; Gruber M
[Ti] Título:Temperature, the benzoylcholine substrate, and fluoride inhibition of pseudocholinesterase.
[So] Source:Can J Anaesth;53(2):208-9, 2006 Feb.
[Is] ISSN:0832-610X
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Benzoilcolina/metabolismo
Butirilcolinesterase/sangue
Fluoretos/farmacologia
Temperatura Ambiente
[Mh] Termos MeSH secundário: Inibidores da Colinesterase/farmacologia
Seres Humanos
Técnicas In Vitro
[Pt] Tipo de publicação:LETTER; COMMENT
[Nm] Nome de substância:
0 (Cholinesterase Inhibitors); 2208-04-0 (Benzoylcholine); EC 3.1.1.8 (Butyrylcholinesterase); Q80VPU408O (Fluorides)
[Em] Mês de entrada:0606
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:060126
[St] Status:MEDLINE



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