The effect of caffeic acid phenethyl ester (CAPE) on metabolic enzymes including acetylcholinesterase, butyrylcholinesterase, glutathione S-transferase, lactoperoxidase, and carbonic anhydrase isoenzymes I, II, IX, and XII.

This work was financed in part by two EU projects of the 7th FP, Metoxia and Dynano. Also, IG and SE would like to extend his sincere appreciation to the Research Chairs Program at King Saud University for providing funding to this research

Rosmarinic acid inhibits some metabolic enzymes including glutathione S-transferase, lactoperoxidase, acetylcholinesterase, butyrylcholinesterase and carbonic anhydrase isoenzymes

Rosmarinic acid (RA) is a natural polyphenol contained in many aromatic plants with promising biological activities. Carbonic anhydrases (CAs, EC 4.2.1.1) are widespread and intensively studied metalloenzymes present in higher vertebrates. Acetylcholinesterase (AChE, E.C. 3.1.1.7) is intimately associated with the normal neurotransmission by catalysing the hydrolysis of acetylcholine to acetate and choline and acts in combination with butyrylcholinesterase (BChE) to remove acetylcholine from the synaptic cleft. Lactoperoxidase (LPO) is an enzyme involved in fighting pathogenic microorganisms, whereas glutathione S-transferases (GSTs) are dimeric proteins present both in prokaryotic and in eukaryotic organisms and involved in cellular detoxification mechanisms. In the present study, the inhibition effects of rosmarinic acid on tumour-associated carbonic anhydrase IX and XII isoenzymes, AChE, BChE, LPO and GST enzymes were evaluated. Rosmarinic acid inhibited these enzymes with K(i)s in the range between micromolar to picomolar. The best inhibitory effect of rosmarinic acid was observed against both AChE and BChE

Identification of chemical components from the Rhizomes of Acorus calamus L. with gas chromatography-tandem mass spectrometry (GC-MS\MS)

In current work our main objective was to search the chemical components of volatiles in AcorusCalamus L. was identified by gas chromatography-tandem mass spectrometry (GC-MS\MS) combined withheadspace (HS) technique. The technique is a very valuable in terms of the extraction yield, sample work uptime, and profiling analysis. According to the our study data, about 78 chemical components were detected fromthe rhizomes of Acorus calamus L. by headspace method. The major components are as follows: 75.8% asarone,79% benzen, 25,8 % trans-?-Ocimene, 20,5% Isocalamendiol, 20,1 % Methyleugenol, 22,6% 3-Carene 17.40%ß-asarone and 17.1% ?-Pinene. In terms of the characteristics of the components contained in this plant and studiesshow that Acorus calamus could be a potential source of novel antibacterial, antioxidant ve anticancer agent

Glutatyon S-Transferaz Enzim Aktivitesi Üzerine Amoksilin ve Vankomisin Hidroklorid Hidratın Etkisi: Bir in vitro çalışma

Glutathione S-transferase (GST) enzymes detoxify a broad spectrum of xenobiotics, includingchemotherapeutic drugs, environmental carcinogens, and endogenous molecules. Glutathione transferases catalyzethe conversion of some metabolites into less toxic substances. Phase II reactions, which often result in detoxification,are conjugation reactions of glutathione through GST enzymes that protect the organism from the attacks of highlyreactive electrophilic substances. Since the GST enzyme can metabolize toxic exogenous compounds, it has beenextensively investigated in mammals. In this study, the GST enzyme was purified in human erythrocytes with aspecific activity of 5.56 EU mg-1 protein and a yield of 2316.0 fold with 65% efficienc. SDS-polyacrylamide gelelectrophoresis was performed to check the purity of the purified enzyme and the molecular mass was determinedto be about 26 kDa. The IC50 and Ki values for amoxycillin and vancomycin hydrochloride drugs on the purifiedGST enzyme were calculated and the type of inhibition was determined. As a result of the inhibition studies, weobserved that these antibiotics inhibited the GST enzyme at low doses.Glutatyon S-transferaz enzimleri kemoterapik ilaçlar, çevresel karsinojenler, endojen moleküller olmaküzere ksenobiyotiklerin geniş bir spektrumunu detoksifiye ederler. Glutatyon transferazlar, bazı metabolitleri dahaaz toksik olan maddelere dönüşmesini katalize eder. Çoğunlukla detoksifikasyonla sonuçlanan faz II reaksiyonlarıarasında organizmayı son derece reaktif elektrofilik maddelerin ataklarından koruyan GST enzimleri aracılığıylagerçekleşen glutatyonun konjugasyon reaksiyonlarıdır. GST enzimi toksik ekzojen bileşikleri metabolizeedebildiğinden dolayı ayrıntılı biçimde memelilerde araştırılmıştır. Bu çalışmada GST enzimi insan eritrositlerinde5.56 EU mg-1 protein spesifik aktiviteyle ve 65 %verimle 2316.0 kat saflaştırıldı. Saflaştırılan enzimin saflığınıkontrol etmek için SDS-poliakrilamid jel elektroforezi yapıldı ve molekül kütlesi yaklaşık 26 kDa olarak belirlendi.Saflaştırılan GST enzimi üzerine inhibisyon etkisi gösteren amoksisilin ve vankomisin hidroklorür için IC50değerleri ve Ki sabitleri hesaplanarak inhibisyon tipleri belirlendi. İnhibisyon çalışmalarının sonucu olarak, buantibiyotiklerin düşük dozlarda GST enzimini inhibe ettiği gözlendi

Karayemiş Meyvesinden (Laurocerasus Officinalis Roem.) Glutatyon S-Transferaz Enziminin Saflaştırılması Ve Karakterizasyonu Ve Bazıpestisitlerin Enzim Aktivitesine İnhibisyon Etkileri

msufbdBu çalışmada karayemiş (Laurucerasus officinalis Roem.)meyvesinden Glutatyon S- Transferaz (EC 2.5.1.18) enzimisaflaştırıldı ve karakterize edildi. Saflaştırma işlemi tek basamakta afinitekromatografisiyle yapıldı. GST enziminin saflığım kontrol etmek için SDS-PAGEelektroforezi uygulandı. Enzim ile ilgilikinetik çalışmalar olarak optimum pH, optimum sıcaklık, optimum iyonik şiddetile indirgenmiş glutatyon (GSH) ve 1- kloro 2, 4- dinitrobenzen (CDNB) için KMve V^ çalışmaları yapıldı. Çalışma sonuçlarına göre GSH için KMve V^değerleri 0.194 mM ve 0.038 EU/ml, CDNB içinKMve V^ değerleri 0.353 mM ve 0.099 EU/ml olarak bulundu. Enzimaktivitesi üzerine bazı pestisitlerin etkisi araştırıldı. Bupestisitlerden; diklorvos, cypermethrin, imidacloprid, fenoxaprop-p-ethyl, glyphosate isopropilamin tuzunun inhibitör özelliği gösterdiği; haloxyfop-p-methyl, lambda- cyhalothrin ve 2, 4-dichlorophenoxyasetic asit dimethylamine tuzunun ise aktivatör olarakdavrandığı tespit edildi.37082

Synthesis, biological evaluation, and bioinformatics analysis of indole analogs on AChE and GST activities

In this article, we aimed to (1) synthesize novel 3-substitue 2-methyl indole analogs, and (2) evaluate their biological activities against Acetylcholinesterase enzyme (AChE) and Glutathione S-transferase enzyme (GST), (3) predict ADMET and pharmacokinetic properties of the 3-substitue 2-methyl indole analogs (4) reveal the possible interactions between 3-substitue 2-methyl indole analogs and selected enzymes. In vitro enzyme inhibition studies revealed the 3-substitue 2-methyl indole analogs exhibited moderate to good inhibitory activities against AChE and GST enzymes. 2-azido-1-(2-methyl-1H-indo1-3-yl) ethanone synthesized was a good inhibitor with the lowest Ki value for both enzymes. Furthermore, a molecular docking study of 3-substitue 2-methyl indole analogs was carried out in the active site of AChE/GST to gain insight into the interaction modes of the synthesized analogs and rationalized structure-activity relationship. The binding energies of the AChE-3substitue 2-methyl indole analogs' complexes were found between -9.3 and -6.0 kcal/mol, and the binding energies of the GST-3-substitue 2-methyl indole analogs' complexes were also found between -11.1 and -7.5 kcal/mol. [GRAPHICS]

Synthesis, Characterization, Enzyme Inhibitory Activity, and Molecular Docking Analysis of a New Series of Thiophene-Based Heterocyclic Compounds

Abstract: 1-Phenyl-3-(thiophen-2-yl)-1H-pyrazole-5-carboxamide derivatives were designed and evaluated for their in vitro enzyme inhibitory activities against acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and glutathione S-transferase (GST). In particular, N,1-diphenyl-3-(thiophen-2-yl)-1H-pyrazole-5-carboxamide (10) was found to be the best AChE inhibitor (Ki = 19.88±3.06 µM), [1-phenyl-3-(thiophen-2-yl)-1H-pyrazole-5-yl](piperidin-1-yl)methanone (8) showed the highest inhibitory activity against BChE (Ki = 13.72±1.12 µM), and (morpholin-4-yl)[1-phenyl-3-(thiophen-2-yl)-1H-pyrazole-5-yl]methanone (7) was found to be the best inhibitor for GST (Ki = 16.44±1.58 µM). Molecular docking studies revealed significant interactions at the enzyme active sites, and compounds 7, 8, and 10 exhibited good binding affinities for GST (–9.7 kcal/mol), BChE (–9.4 kcal/mol), and AChE (–9.3 kcal/mol), respectively. The results of the present study have good potential to contribute further structural modifications and pharmacological studies related to enzyme inhibitors. © 2021, Pleiades Publishing, Ltd

The effects of some antibiotics from cephalosporin groups on the acetylcholinesterase and butyrylcholinesterase enzymes activities in different tissues of rats

In our study, it was aimed to investigate the effects of cefazolin, cefuroxime, and cefoperazon injected to rats on acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) enzyme activities in the heart, brain, eye, liver, and kidney tissues of rats. Liver AChE activity at the 1st and 3rd hours of cefuroxime groups was higher than the control group at the same time (p <.05). The AChE activity of the heart tissue decreased in the cefazolin group compared to the control group at the same hour, whereas it increased in the cefuroxime group (p <.05). AChE activities of kidney tissue of cefazolin and cefuroxime groups were lower than those of the same control group on the 3rd and started to increase on the next hours (p <.05). BChE activity is measured in tissues increased within the first three hours and decreased significantly within the first hour in the cefoperazone group (p <.05)