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Arylesterase

Arylesterase is an enzyme that plays a crucial role in the hydrolysis of aromatic esters, such as phenyl acetate.
It is primarily found in the liver and serum, and its activity is often used as a marker for organophosphate exposure and liver function.
Arylesterase is involved in the detoxification of various xenobiotics and plays a part in the metabolism of certain drugs.
Understanding the regulation and function of arylesterase is important for research in toxicology, pharmacology, and related fields.
Accurate and reproducibke experimental protocols are essential for studying this enzyme, and tools like PubCompare.ai can help researchers identify the most reliable protocols from the scientific literature, pre-prints, and patents.

Most cited protocols related to «Arylesterase»

1
Accurate Annotation of Biologically Relevant Ligands
Cited 45 times
An accurate annotation of the biological relevance of the ligand entries is essential to the BioLiP data collection. A ligand molecule present in a target protein is considered as biologically relevant if it interacts with the protein and plays certain biological roles, such as inhibitor, activator and substrate analog (3 (link),7 (link)). To guarantee the high accuracy and speed, we developed a composite automated and manual procedure as outlined in Figure 1. First, an automated four-step hierarchical procedure is used to verify the biological relevance of a ligand. After the automated procedure is completed, a careful manual check is performed to eliminate possible false positives, which can occur for entries with the commonly used crystallization additives.
To speed up the annotation procedure as well as increase the accuracy, we manually pre-collected a set of 353 suspiciously non-biological ligands, which are frequently used for the protein structure determination (including crystallization additives, non-biological ions, heavy metal and so on.) To generate this list, we first collected all ligands that are observed for >20 times in known protein structures. This list was refined further by analyzing the possible biological role of these ligands, e.g. a ligand is removed from the list if it is found to have biological relevance in the related literature of the structure file or is present in the KEGG database (26 (link)). This list is used to help assess the biological relevance of each ligand in PDB automatically (Figure 1) and is available at http://zhanglab.ccmb.med.umich.edu/BioLiP/ligand_list.
The automated filtering procedure consists of four steps:

First, if the candidate ligand is in the artifact list and appears >15 times in the same structure file, then it is likely to be crystallization additive and is considered as biologically irrelevant.

Second, the contacts between the receptor and ligand atoms are computed. The record ‘REMARK 350’ in the asymmetric unit files is used to exclude crystallization neighbors. This record presents which chains of the structure should be put together and the mathematical transformations (i.e. rotation and translation matrices) operated on each chain to generate biomolecules (i.e. biological unit files). The contacts between two chains are evaluated only when both chains are used to generate a biomolecule. For a receptor residue, if the closest atomic distance between the residue and the ligand is within certain distance cutoff, then the residue is defined as a ligand-binding site residue. The cutoff is set to be 0.5 plus the sum of the Van der Waal’s radius of the two atoms under investigation (7 (link)). If the number of binding site residues (i.e. number of contacts) is less than two or all the binding site residues are consecutive, it is deemed to be biologically irrelevant because most biological relevant ligands are usually tethered by multiple residues, which are further apart in the sequence space.

Third, if the ligand is not present in the artifact list, then it is considered as biologically relevant and kept in the pipeline for further manual verifications.

Fourth, the PubMed abstract is used to filter out biologically irrelevant ligands. If the ligand is in the artifact list, the simplest way is to treat it as biologically irrelevant and discard it. But this will miss some ligands (false negatives) that are indeed biologically relevant in some cases. For instance, the ligand molecule ‘glycerol’ (with ligand ID ‘GOL’) is one of the most frequently used crystallization additives and it is thus regarded as biologically irrelevant by many existing databases. However, this ligand can have a biological role in some proteins. For example, the ligand molecule glycerol binds to the protein ‘enzyme diol dehydratase’ (PDB ID: 3AUJ) with binding affinity Km = 1.2 ± 0.02 mM with its biological role described as ‘glycerol is bound to the substrate binding site in the (β/α)8 or TIM barrel of the diol dehydratase α subunit’ in (27 (link)). Thus, this ligand is considered as biologically relevant for this protein and added to BioLiP. We found that if a ligand present in a protein has its relevant biological role, it is often mentioned in the PubMed abstract. Based on such observation, we propose to use the PubMed abstract as an additional filter. To this end, the chemical names/synonyms of the ligand (curated from ChEBI, PubChem and PDB databases) are compared with the PubMed abstract. If there is no hit in this comparison procedure, the ligand is deemed to be biologically irrelevant. Otherwise, the ligand is possible to be biologically relevant, which remains to be verified by hand in the next step.

Finally, the manual verification is performed to check for suspicious or ambiguous entries, which are referred to those entries related with the commonly used crystallization additives, such as glycerol, ethanol, methanol, 2-propanol, ethylene glycol, hexylene glycol and polyethylene glycol. Ligands filtered from the above four steps can sometimes still be false positives, which is usually caused by unexpected match between the ligand names/synonyms and the PubMed abstract. In the same example of the ligand ‘glycerol’, it has the synonym ‘glycyl alcohol’, which leads to an unexpected match of the term ‘alcohol’ for the protein ‘arylesterase’ (PDB ID: 3HI4). Therefore, manual verification for ligands that are commonly used as crystallization additives is necessary to ensure the quality of BioLiP. Currently, we do this manual verification mainly by reading the original literatures and consulting other secondary databases. In the current version of BioLiP, manual verifications helped us to remove ∼12 500 entries that were false positives and we added ∼3000 entries that would have been missed by using the automated procedure alone.

Yang J., Roy A, & Zhang Y. (2012). BioLiP: a semi-manually curated database for biologically relevant ligand–protein interactions. Nucleic Acids Research, 41(Database issue), D1096-D1103.
Publication 2012
arylesterase Binding Sites Biopharmaceuticals Crystallization Enzymes Ethanol Glycerin Glycol, Ethylene hexylene glycol Ions Isopropyl Alcohol Ligands Metals, Heavy Methanol Polyethylene Glycols Propanediol Dehydratase Proteins Protein Subunits Protein Targeting, Cellular Radius Staphylococcal Protein A
2
Spectrophotometric Assay for PON1 Phenotyping
Cited 8 times

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Publication 2008
3
Paraoxonase-1 Activity Assay Protocol
Cited 6 times
Paraoxonase-1 paraoxonase activity was analysed by a kinetic, semi-automated method. Briefly, we used paraoxon (O,O-diethyl-O-p-nitrophenyl-phosphate, Sigma, Hungary) as a substrate, and the generation of 4-nitrophenol was measured on a microtiter plate (Greiner Bio-One GmbH, Frickenhausen, Germany). Serum of 15 μl was mixed with 285 μl Tris-HCl buffer (100 mmol/l, pH = 8.0) containing 2 mmol/l CaCl2 and 5.5 mmol/l paraoxon. The absorbance was monitored at 405 nm (25°C), in every minute for 6 min. by a Beckman Coulter DTX880 Plate Reader (Beckman Coulter, Brea, CA, USA) equipped with a multimode detector. Enzyme activity was calculated using the molar extinction coefficient 17,600 M/cm. Paraoxonase activity is expressed as units per litre of serum, where 1 unit equals 1 μmol of substrate hydrolysed per minute.
Paraoxonase-1 arylesterase activity was assayed containing 1 mM phenylacetate substrate (Sigma-Aldrich, Budapest, Hungary) in 20 mM Tris-HCl, pH = 8.0. The reaction was started by adding the serum and the absorbance was monitored at 270 nm. Blanks were included to correct for the spontaneous hydrolysis of phenylacetate. Enzyme activity was calculated using the molar extinction coefficient 1310 M/cm. Arylesterase activity is expressed in U/l; 1 U is defined as 1 μmol phenylacetate hydrolysed per minute.
Fülöp P., Seres I., Lőrincz H., Harangi M., Somodi S, & Paragh G. (2014). Association of chemerin with oxidative stress, inflammation and classical adipokines in non-diabetic obese patients. Journal of Cellular and Molecular Medicine, 18(7), 1313-1320.
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Publication 2014
Aryldialkylphosphatase arylesterase enzyme activity Extinction, Psychological Hydrolysis Kinetics Molar Nitrophenols Paraoxon Paraoxonase 1 phenyl acetate Serum Tromethamine
4
Lipoprotein Profiling by NMR Spectroscopy
Cited 4 times
Blood serum lipoproteins were measured on a Bruker 600 MHz Avance Neo NMR spectrometer using the Bruker IVDr lipoprotein subclass analysis protocol. Serum samples were thawed, and 330 µL of each sample mixed with 330 µL of Bruker serum buffer (Bruker, Rheinstetten, Germany). The samples were mixed gently, and 600 µL of the mixed sample were transferred into a 5 mm SampleJet rack tube (Bruker). Proton spectra were obtained at a constant temperature of 310 K using a standard nuclear Overhauser effect spectroscopy (NOESY) pulse sequence (Bruker: noesygppr1d), a Carr–Purcedll–Meiboom–Gill (CPMG) pulse sequence with presaturation during the relaxation delay (Bruker: cpmgpr1d) to achieve water suppression, and a standard 2D J-resolved (JRES) pulse sequence (Bruker: jresgpprqf). Data analysis was carried out using the Bruker IVDr LIpoprotein Subclass Analysis (B.I.LISATM, Bruker, Rheinstetten, Germany) method.
Schilcher I., Stadler J.T., Lechleitner M., Hrzenjak A., Berghold A., Pregartner G., Lhomme M., Holzer M., Korbelius M., Reichmann F., Springer A., Wadsack C., Madl T., Kratky D., Kontush A., Marsche G, & Frank S. (2021). Endothelial Lipase Modulates Paraoxonase 1 Content and Arylesterase Activity of HDL. International Journal of Molecular Sciences, 22(2), 719.
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Publication 2021
Buffers Gills Lipoproteins Protons Pulse Rate Serum Spectrum Analysis
5
Spectrophotometric Determination of Paraoxonase and Arylesterase Activities
Cited 3 times
Paraoxonase activity was determined spectrophotometrically using paraoxon (O, O-diethyl-o-p-nitro-phenylphosphate; Sigma Chemical Co) as the substrate and measured by increases in the absorbance at 412 nm due to the formation of 4-nitrophenol as already described [23 (link)]. Briefly, the activity was measured at 25°C by adding 50 μl of serum to 1 ml Tris-HCl buffer (100 nM at pH 8.0) containing 2 mM CaCl2 and 5.5 mM of paraoxon. The rate of generation of 4-nitrophenol was determined at 412 nm with a spectrophotometer (Techcomp 8500 II UV/VIS, China). PON1 activity is expressed in U/l serum. One unit of PON1 activity was defined as 1 nmol of 4-nitrophenol formed per minute under the above assay conditions.
Arylesterase activity was also measured spectrophotometrically using phenylacetate (Sigma Co, London, UK) as the substrate. The phenol formed after the addition of a 40-fold diluted serum sample was measured spectrophotometrically at 217 nm following an established procedure [24 (link)]. The activity of ARE was expressed in kU/l serum. One unit was defined as the enzyme quantity that disintegrates 1 nmol phenylacetate per minute.
Elkiran E.T., Mar N., Aygen B., Gursu F., Karaoglu A, & Koca S. (2007). Serum paraoxonase and arylesterase activities in patients with lung cancer in a Turkish population. BMC Cancer, 7, 48.
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Publication 2007
Aryldialkylphosphatase arylesterase Biological Assay Enzymes Nitrophenols Paraoxon Phenol phenyl acetate phenylphosphate PON1 protein, human Serum Tromethamine

Most recents protocols related to «Arylesterase»

1
Arylesterase Activity Assay for PON-1 Enzyme
Not available on PMC !
Sigma (Saint Louis, MO, USA) supplied phenylacetate, which serves as a substrate for the PON-1 enzyme. In order to measure the arylesterase activity of this enzyme in serum, the procedure proposed by Bobin-Dubigeon et al. (19) has been recruited. The method comprises measuring phenylacetate hydrolysis as an indicator of enzyme activity. Specifically, 100 μL of serum was mixed with 2 mM calcium chloride, 2 mM substrate, and 100 mM TRIS-HCl (pH 8.0), followed by incubation at 37 °C for three minutes. The hydrolysis of the substrate was subsequently determined at 270 nm.
Samareh A., Pourghadamyari H., Nemtollahi M.H., Ebrahimi H.A., Norouzmahani M.E., & Asadikaram G. (2024). The Impact of Pesticides on Parkinson's Disease; A Case-Control Study.
Publication 2024
2
Plasma AE Activity Determination
Not available on PMC !
AE activity was determined in plasma according to the method of Macho-González et al. 40 Simulated body fluid was used as 16.73 kJ g -1 (4.0 kcal g -1 ), fat 37.65 kJ g -1 (9.0 kcal g -1 ), and protein 16.73 kJ g -1 (4.0 kcal g -1 ).
Hernández-Martín M., Macho-González A., Garcimartín A., López-Oliva M.E., Bocanegra A., Redondo-Castillejo R., Bastida S., Benedí J, & Sánchez-Muniz F.J. (2024). Silicon-enriched meat positively improves plasma lipidaemia and lipoproteinaemia, LDLr, and insulin capability and the signalling pathway induced by an atherogenic diet in late-stage type 2 diabetes mellitus rats. Food & function, 15(3).
Publication 2024
3
Measuring PON1 Arylesterase Activity
The arylesterase (ARE) activity of PON1 was measured using phenyl acetate as the substrate [28 (link)]. In brief, the assays were conducted in a final volume of 250 μL, comprising 5 μL of serum diluted 1:50, or 5 μL of cortical homogenate, 1 mM phenyl acetate, 100 mM Tris-HCl, and 2 mM CaCl2, pH 8.0. The rate of phenol formation resulting from phenyl acetate hydrolysis was determined by recording the increase in absorbance at 270 nm over 5 min at 25 °C using a microtiter plate reader (Spark, Tecan Trading AG). The serum ARE activity of PON1 was normalized with the apoA-I concentration and expressed as kU/mg of apoA-I, where one U represents the activity catalyzing the formation of one μmol of phenyl acetate per minute. The ARE activity of PON1 in cortical homogenates was normalized with the protein concentration and expressed as U/g of protein.
Lymperopoulos D., Dedemadi A.G., Voulgari M.L., Georgiou E., Dafnis I., Mountaki C., Panagopoulou E.A., Karvelas M., Chiou A., Karathanos V.T, & Chroni A. (2024). Corinthian Currants Promote the Expression of Paraoxonase-1 and Enhance the Antioxidant Status in Serum and Brain of 5xFAD Mouse Model of Alzheimer’s Disease. Biomolecules, 14(4), 426.
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Publication 2024
4
Arylesterase Activity of Recombinant PON1
The arylesterase activity of recombinant PON1 was measured either in the absence or presence of currant extract at various concentrations (1–10 μg GAE/mL). As the enzyme source, we used 50 µL of cell medium of HEK293 cells transfected, in a 12-well plate, with the pcDNA3.1+/C-(K)-DYK/PON1 vector and cultured in the absence of currant extract, as described above. The arylesterase activity of recombinant PON1 was determined by monitoring the increase in absorbance, following phenyl acetate hydrolysis, at 270 nm for 10 min.
Lymperopoulos D., Dedemadi A.G., Voulgari M.L., Georgiou E., Dafnis I., Mountaki C., Panagopoulou E.A., Karvelas M., Chiou A., Karathanos V.T, & Chroni A. (2024). Corinthian Currants Promote the Expression of Paraoxonase-1 and Enhance the Antioxidant Status in Serum and Brain of 5xFAD Mouse Model of Alzheimer’s Disease. Biomolecules, 14(4), 426.
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Publication 2024
5
Histological Analysis of Lamb Skin
Not available on PMC !
The potassium concentration in blood samples was determined by interpolation using galvanometer readings in a Zeiss-Jena III flame photometer. The analysis of the obtained blood samples was carried out according to the method of N.S. Poluektova [8] .
The enzymatic activity of O-diphenoloxidase was determined according to the method of M.T. Taranova [9] .
Arylesterase activity was detected in the blood serum of animals according to the method of E. M. Tucker Y. Suzuki C. Stormont. [eleven] .
The activity of tyrosine aminotransferase was detected in urine samples of experimental sheep according to the method of E.F. Davidenkov and I.S. Lieberman [4] .
When determining the histological parameters of the skin by biopsy in lambs of 1-2 days of age of various colors, samples were taken in the middle part of the back. Histological samples are described according to the method developed by the Institute of Animal Morphology named after A.A. Severtsev of the Academy of Sciences of the Russian Federation (E.K. Merkuryeva) [5] .
At the same time, the thickness of the skin and its layers (epidermal, polar, reticular), density (primary, secondary) and the total number of follicles per 1 mm2 were determined.
Lambs of various colors were individually graded according to the "Instructions for the evaluation of Karakul lambs with the basics of breeding" [10] .
Omonov M. (2024). Influence of biologically active substances of blood of Karakulsan sheep rim on preservation of gene pool and productivity. E3S Web of Conferences, 494, 04004-04004.
Publication 2024

Top products related to «Arylesterase»

1
Phenylacetate by Merck Group
Sourced in United States, Hungary
Phenylacetate is a chemical compound used in various laboratory applications. It is a colorless liquid with a characteristic odor. Phenylacetate is commonly used as a reagent in organic synthesis, analytical chemistry, and biochemical research.
2
Paraoxon by Merck Group
Sourced in United States, Germany, Hungary, Israel, United Kingdom
Paraoxon is a laboratory reagent used in analytical chemistry and biochemical research. It is a chemical compound that can be utilized as a substrate or analytical standard in various assays and investigations. The core function of Paraoxon is to serve as a tool for scientific analysis and experimentation, without interpretation of its intended use.
3
Phenylacetate substrate by Merck Group
Sourced in Hungary
Phenylacetate substrate is a chemical compound used in analytical and research laboratory settings. It serves as a substrate for various enzymatic reactions and assays. The product provides a standardized material for consistent and reliable experimental procedures, but its specific applications and intended uses are not included in this factual description.
4
Du 640 by Beckman Coulter
Sourced in United States, Germany, Italy, United Kingdom
The DU 640 is a UV-Vis spectrophotometer designed for routine laboratory analysis. It features a dual-beam optical system with a wavelength range of 190 to 1100 nanometers. The instrument is capable of performing absorbance, transmittance, and concentration measurements.
5
Superose 6b column by GE Healthcare
Sourced in United States
The Superose 6B column is a gel filtration chromatography column used for the size-based separation of proteins and other macromolecules. It is designed to provide efficient and high-resolution separation of molecules with a molecular weight range of 5,000 to 500,000 Daltons.
6
Uv transparent 96 well plate by Merck Group
The UV-transparent 96-well plate is a laboratory equipment designed for use in various scientific applications. It features a transparent material that allows ultraviolet (UV) light to pass through, enabling UV-based analysis and measurements within the well plate format.
7
Spss statistics for windows version 18 by IBM
Sourced in United States
SPSS Statistics for Windows, version 18.0 is a statistical software package developed by IBM. It is designed to analyze and manage data, and provides a wide range of statistical and analytical tools for researchers, analysts, and data scientists.
8
Infinite m200 by Tecan
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The Infinite M200 is a multi-mode microplate reader that provides high-performance absorbance, fluorescence, and luminescence detection. It offers precise and versatile measurement capabilities for a wide range of applications in life science research and drug discovery.
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Synergy ht by Agilent Technologies
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The Synergy HT is a multi-mode microplate reader from Agilent Technologies. It is designed to perform absorbance, fluorescence, and luminescence measurements on microplates. The Synergy HT provides reliable data for a wide range of applications, including cell-based assays, ELISA, and other microplate-based experiments.
10
Spectramax 190 plate reader by Molecular Devices
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The SpectraMax 190 plate reader is a versatile spectrophotometric instrument designed for absorbance-based assays. It can accurately measure the optical density of samples in a 96-well microplate format. The device is capable of performing a range of common laboratory assays, such as protein quantification, enzyme activity determination, and cell-based assays.

More about "Arylesterase"

Arylesterase, also known as paraoxonase, is a crucial enzyme that plays a pivotal role in the hydrolysis of aromatic esters, such as phenyl acetate.
It is predominantly found in the liver and serum, and its activity is frequently utilized as a marker for organophosphate exposure and liver function assessment.
This enzyme is integral to the detoxification of various xenobiotics and plays a significant part in the metabolism of certain drugs.
Understanding the regulation and function of arylesterase is crucial for research in toxicology, pharmacology, and related fields.
Accurate and reproducible experimental protocols are essential for studying this enzyme, and tools like PubCompare.ai can help researchers identify the most reliable protocols from the scientific literature, pre-prints, and patents.
Phenylacetate is a common substrate used in arylesterase activity assays, and paraoxon is a well-known organophosphate inhibitor of the enzyme.
Techniques like DU 640 spectrophotometry, Superose 6B column chromatography, and UV-transparent 96-well plate assays have been employed to measure arylesterase activity.
Statistical analysis tools, such as SPSS Statistics for Windows, version 18.0, and plate readers like Infinite M200, Synergy HT, and SpectraMax 190, have been utilized to analyze and interpret the data.
By leveraging the insights from PubCompare.ai, researchers can enhance their arylesterase studies, leading to more reproducibile and accurate experimental outcomes.