Cholinesterase from the common prawn ( Palaemon serratus) eyes: Catalytic properties and sensitivity to organophosphate and carbamate compounds
The main purpose of this study was to describe the kinetic properties of the cholinesterase (ChE) enzyme present in the eyes of the prawn Palaemon serratus, an abundant, ecological and commercially relevant species of European coastal environments. The obtained results suggest that the studied enzym...
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| Veröffentlicht in: | Aquatic toxicology 2006-05, Vol.77 (4), p.412-421 |
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| creator | Frasco, Manuela F. Fournier, Didier Carvalho, Félix Guilhermino, Lúcia |
| description | The main purpose of this study was to describe the kinetic properties of the cholinesterase (ChE) enzyme present in the eyes of the prawn
Palaemon serratus, an abundant, ecological and commercially relevant species of European coastal environments. The obtained results suggest that the studied enzyme is a ChE and not a non-specific esterase, due to its apparent affinity for choline esters and the high sensitivity to eserine sulphate. This ChE displays a distinct preference for the substrate acetylthiocholine, showing a triphasic behaviour, with activation at low concentrations and inhibition by excess of substrate. Moreover, irreversible ChE inhibition by several organophosphate and carbamate compounds was characterized. All the irreversible inhibitions were homogeneous following a second-order rate reaction. The bimolecular rate constant (
k
i
) values of ChE inhibition by the tested pesticides were also estimated and compared with available data from other invertebrate and vertebrate species. In conclusion, the results of the present study showed that prawn eyes possess only one ChE with typical properties of acetylcholinesterase, which is highly sensitive to the tested anti-cholinesterase compounds. |
| doi_str_mv | 10.1016/j.aquatox.2006.01.011 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_hal_p</sourceid><recordid>TN_cdi_hal_primary_oai_HAL_hal_00120643v1</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0166445X06000415</els_id><sourcerecordid>20898100</sourcerecordid><originalsourceid>FETCH-LOGICAL-c428t-b0ec71562904776fa07a48b5968801b8ccae48e5b3c7a59520fa34dbbe7fc5c23</originalsourceid><addsrcrecordid>eNqF0d2K1DAUB_AiijuuPoKaG8W9mPEk_Ur3RpZBXWFAQRe8C6fp6U6Gtukm6eg8ha9s6gzu5YZASPglOck_SV5yWHHgxfvdCu8mDPb3SgAUK-Cx80fJgsuyWvKcZ4-TRXTFMsvyn2fJM-93EJvIqqfJGS-yqkyrYpH8WW9tZwbygRx6Yq2zPQtbYtr2vR3Y6PDXwN6xb9ghzQuenMMw-QtGB_KXbI0Bu0MwOlI7kguGPMOhiXDwJpi9CQcWLLPuFgc7bq0ftxjoH9HoauznWbxttNPQ-OfJkxY7Ty9O43ly8-njj_X1cvP185f11WapMyHDsgbSJc8LUUFWlkWLUGIm67wqpAReS62RMkl5neoS8yoX0GKaNXVNZatzLdLz5OJ47hY7NTrTozsoi0ZdX23UvAbABRRZuufRvj3a-MK7KX6V6o3X1HU4kJ28EiAryQEehDzWKmSRRpgfoXbWe0ft_xI4qDletVOneNUcrwIe-1zJq9MFU91Tc7_rlGcEb04AvcaudTho4-9dGT9LQhnd66Nr0Sq8ddHcfBfAU-AgeSVm8eEoKKawN-SU14YGTY1xpINqrHmg2L-dB9HF</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>14772863</pqid></control><display><type>article</type><title>Cholinesterase from the common prawn ( Palaemon serratus) eyes: Catalytic properties and sensitivity to organophosphate and carbamate compounds</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>Frasco, Manuela F. ; Fournier, Didier ; Carvalho, Félix ; Guilhermino, Lúcia</creator><creatorcontrib>Frasco, Manuela F. ; Fournier, Didier ; Carvalho, Félix ; Guilhermino, Lúcia</creatorcontrib><description>The main purpose of this study was to describe the kinetic properties of the cholinesterase (ChE) enzyme present in the eyes of the prawn
Palaemon serratus, an abundant, ecological and commercially relevant species of European coastal environments. The obtained results suggest that the studied enzyme is a ChE and not a non-specific esterase, due to its apparent affinity for choline esters and the high sensitivity to eserine sulphate. This ChE displays a distinct preference for the substrate acetylthiocholine, showing a triphasic behaviour, with activation at low concentrations and inhibition by excess of substrate. Moreover, irreversible ChE inhibition by several organophosphate and carbamate compounds was characterized. All the irreversible inhibitions were homogeneous following a second-order rate reaction. The bimolecular rate constant (
k
i
) values of ChE inhibition by the tested pesticides were also estimated and compared with available data from other invertebrate and vertebrate species. In conclusion, the results of the present study showed that prawn eyes possess only one ChE with typical properties of acetylcholinesterase, which is highly sensitive to the tested anti-cholinesterase compounds.</description><identifier>ISSN: 0166-445X</identifier><identifier>EISSN: 1879-1514</identifier><identifier>DOI: 10.1016/j.aquatox.2006.01.011</identifier><identifier>PMID: 16497396</identifier><identifier>CODEN: AQTODG</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Acetylthiocholine - metabolism ; animal models ; Animal, plant and microbial ecology ; Animals ; Applied ecology ; Biochemistry, Molecular Biology ; Biological and medical sciences ; Biomarker ; biomarkers ; carbamate pesticides ; Carbamates - pharmacokinetics ; Carbamates - pharmacology ; Cholinesterase ; Cholinesterase Inhibitors - pharmacology ; Cholinesterases - drug effects ; Cholinesterases - metabolism ; Ecotoxicology, biological effects of pollution ; enzyme activation ; enzyme activity ; enzyme inhibitors ; Estuarine invertebrate ; Eye - drug effects ; Eye - enzymology ; eyes ; Fundamental and applied biological sciences. Psychology ; General aspects ; Life Sciences ; Organophosphate and carbamate pesticides ; Organophosphates - pharmacokinetics ; Organophosphates - pharmacology ; organophosphorus pesticides ; Palaemon serratus ; Palaemonidae - drug effects ; Palaemonidae - enzymology ; Pesticides - pharmacokinetics ; Pesticides - pharmacology ; shrimp ; Substrate Specificity ; Thiocholine - analogs & derivatives ; Thiocholine - metabolism ; toxicity testing ; Water Pollutants, Chemical - pharmacokinetics ; Water Pollutants, Chemical - pharmacology</subject><ispartof>Aquatic toxicology, 2006-05, Vol.77 (4), p.412-421</ispartof><rights>2006 Elsevier B.V.</rights><rights>2006 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c428t-b0ec71562904776fa07a48b5968801b8ccae48e5b3c7a59520fa34dbbe7fc5c23</citedby><cites>FETCH-LOGICAL-c428t-b0ec71562904776fa07a48b5968801b8ccae48e5b3c7a59520fa34dbbe7fc5c23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.aquatox.2006.01.011$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,780,784,885,3548,27923,27924,45994</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17776807$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16497396$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00120643$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Frasco, Manuela F.</creatorcontrib><creatorcontrib>Fournier, Didier</creatorcontrib><creatorcontrib>Carvalho, Félix</creatorcontrib><creatorcontrib>Guilhermino, Lúcia</creatorcontrib><title>Cholinesterase from the common prawn ( Palaemon serratus) eyes: Catalytic properties and sensitivity to organophosphate and carbamate compounds</title><title>Aquatic toxicology</title><addtitle>Aquat Toxicol</addtitle><description>The main purpose of this study was to describe the kinetic properties of the cholinesterase (ChE) enzyme present in the eyes of the prawn
Palaemon serratus, an abundant, ecological and commercially relevant species of European coastal environments. The obtained results suggest that the studied enzyme is a ChE and not a non-specific esterase, due to its apparent affinity for choline esters and the high sensitivity to eserine sulphate. This ChE displays a distinct preference for the substrate acetylthiocholine, showing a triphasic behaviour, with activation at low concentrations and inhibition by excess of substrate. Moreover, irreversible ChE inhibition by several organophosphate and carbamate compounds was characterized. All the irreversible inhibitions were homogeneous following a second-order rate reaction. The bimolecular rate constant (
k
i
) values of ChE inhibition by the tested pesticides were also estimated and compared with available data from other invertebrate and vertebrate species. In conclusion, the results of the present study showed that prawn eyes possess only one ChE with typical properties of acetylcholinesterase, which is highly sensitive to the tested anti-cholinesterase compounds.</description><subject>Acetylthiocholine - metabolism</subject><subject>animal models</subject><subject>Animal, plant and microbial ecology</subject><subject>Animals</subject><subject>Applied ecology</subject><subject>Biochemistry, Molecular Biology</subject><subject>Biological and medical sciences</subject><subject>Biomarker</subject><subject>biomarkers</subject><subject>carbamate pesticides</subject><subject>Carbamates - pharmacokinetics</subject><subject>Carbamates - pharmacology</subject><subject>Cholinesterase</subject><subject>Cholinesterase Inhibitors - pharmacology</subject><subject>Cholinesterases - drug effects</subject><subject>Cholinesterases - metabolism</subject><subject>Ecotoxicology, biological effects of pollution</subject><subject>enzyme activation</subject><subject>enzyme activity</subject><subject>enzyme inhibitors</subject><subject>Estuarine invertebrate</subject><subject>Eye - drug effects</subject><subject>Eye - enzymology</subject><subject>eyes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects</subject><subject>Life Sciences</subject><subject>Organophosphate and carbamate pesticides</subject><subject>Organophosphates - pharmacokinetics</subject><subject>Organophosphates - pharmacology</subject><subject>organophosphorus pesticides</subject><subject>Palaemon serratus</subject><subject>Palaemonidae - drug effects</subject><subject>Palaemonidae - enzymology</subject><subject>Pesticides - pharmacokinetics</subject><subject>Pesticides - pharmacology</subject><subject>shrimp</subject><subject>Substrate Specificity</subject><subject>Thiocholine - analogs & derivatives</subject><subject>Thiocholine - metabolism</subject><subject>toxicity testing</subject><subject>Water Pollutants, Chemical - pharmacokinetics</subject><subject>Water Pollutants, Chemical - pharmacology</subject><issn>0166-445X</issn><issn>1879-1514</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0d2K1DAUB_AiijuuPoKaG8W9mPEk_Ur3RpZBXWFAQRe8C6fp6U6Gtukm6eg8ha9s6gzu5YZASPglOck_SV5yWHHgxfvdCu8mDPb3SgAUK-Cx80fJgsuyWvKcZ4-TRXTFMsvyn2fJM-93EJvIqqfJGS-yqkyrYpH8WW9tZwbygRx6Yq2zPQtbYtr2vR3Y6PDXwN6xb9ghzQuenMMw-QtGB_KXbI0Bu0MwOlI7kguGPMOhiXDwJpi9CQcWLLPuFgc7bq0ftxjoH9HoauznWbxttNPQ-OfJkxY7Ty9O43ly8-njj_X1cvP185f11WapMyHDsgbSJc8LUUFWlkWLUGIm67wqpAReS62RMkl5neoS8yoX0GKaNXVNZatzLdLz5OJ47hY7NTrTozsoi0ZdX23UvAbABRRZuufRvj3a-MK7KX6V6o3X1HU4kJ28EiAryQEehDzWKmSRRpgfoXbWe0ft_xI4qDletVOneNUcrwIe-1zJq9MFU91Tc7_rlGcEb04AvcaudTho4-9dGT9LQhnd66Nr0Sq8ddHcfBfAU-AgeSVm8eEoKKawN-SU14YGTY1xpINqrHmg2L-dB9HF</recordid><startdate>20060525</startdate><enddate>20060525</enddate><creator>Frasco, Manuela F.</creator><creator>Fournier, Didier</creator><creator>Carvalho, Félix</creator><creator>Guilhermino, Lúcia</creator><general>Elsevier B.V</general><general>Elsevier Science</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7ST</scope><scope>C1K</scope><scope>SOI</scope><scope>7QH</scope><scope>7TN</scope><scope>7TV</scope><scope>7U7</scope><scope>7UA</scope><scope>F1W</scope><scope>H95</scope><scope>H97</scope><scope>L.G</scope><scope>1XC</scope></search><sort><creationdate>20060525</creationdate><title>Cholinesterase from the common prawn ( Palaemon serratus) eyes: Catalytic properties and sensitivity to organophosphate and carbamate compounds</title><author>Frasco, Manuela F. ; Fournier, Didier ; Carvalho, Félix ; Guilhermino, Lúcia</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c428t-b0ec71562904776fa07a48b5968801b8ccae48e5b3c7a59520fa34dbbe7fc5c23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Acetylthiocholine - metabolism</topic><topic>animal models</topic><topic>Animal, plant and microbial ecology</topic><topic>Animals</topic><topic>Applied ecology</topic><topic>Biochemistry, Molecular Biology</topic><topic>Biological and medical sciences</topic><topic>Biomarker</topic><topic>biomarkers</topic><topic>carbamate pesticides</topic><topic>Carbamates - pharmacokinetics</topic><topic>Carbamates - pharmacology</topic><topic>Cholinesterase</topic><topic>Cholinesterase Inhibitors - pharmacology</topic><topic>Cholinesterases - drug effects</topic><topic>Cholinesterases - metabolism</topic><topic>Ecotoxicology, biological effects of pollution</topic><topic>enzyme activation</topic><topic>enzyme activity</topic><topic>enzyme inhibitors</topic><topic>Estuarine invertebrate</topic><topic>Eye - drug effects</topic><topic>Eye - enzymology</topic><topic>eyes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General aspects</topic><topic>Life Sciences</topic><topic>Organophosphate and carbamate pesticides</topic><topic>Organophosphates - pharmacokinetics</topic><topic>Organophosphates - pharmacology</topic><topic>organophosphorus pesticides</topic><topic>Palaemon serratus</topic><topic>Palaemonidae - drug effects</topic><topic>Palaemonidae - enzymology</topic><topic>Pesticides - pharmacokinetics</topic><topic>Pesticides - pharmacology</topic><topic>shrimp</topic><topic>Substrate Specificity</topic><topic>Thiocholine - analogs & derivatives</topic><topic>Thiocholine - metabolism</topic><topic>toxicity testing</topic><topic>Water Pollutants, Chemical - pharmacokinetics</topic><topic>Water Pollutants, Chemical - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Frasco, Manuela F.</creatorcontrib><creatorcontrib>Fournier, Didier</creatorcontrib><creatorcontrib>Carvalho, Félix</creatorcontrib><creatorcontrib>Guilhermino, Lúcia</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Environment Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Environment Abstracts</collection><collection>Aqualine</collection><collection>Oceanic Abstracts</collection><collection>Pollution Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Water Resources Abstracts</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 3: Aquatic Pollution & Environmental Quality</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Aquatic toxicology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Frasco, Manuela F.</au><au>Fournier, Didier</au><au>Carvalho, Félix</au><au>Guilhermino, Lúcia</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cholinesterase from the common prawn ( Palaemon serratus) eyes: Catalytic properties and sensitivity to organophosphate and carbamate compounds</atitle><jtitle>Aquatic toxicology</jtitle><addtitle>Aquat Toxicol</addtitle><date>2006-05-25</date><risdate>2006</risdate><volume>77</volume><issue>4</issue><spage>412</spage><epage>421</epage><pages>412-421</pages><issn>0166-445X</issn><eissn>1879-1514</eissn><coden>AQTODG</coden><abstract>The main purpose of this study was to describe the kinetic properties of the cholinesterase (ChE) enzyme present in the eyes of the prawn
Palaemon serratus, an abundant, ecological and commercially relevant species of European coastal environments. The obtained results suggest that the studied enzyme is a ChE and not a non-specific esterase, due to its apparent affinity for choline esters and the high sensitivity to eserine sulphate. This ChE displays a distinct preference for the substrate acetylthiocholine, showing a triphasic behaviour, with activation at low concentrations and inhibition by excess of substrate. Moreover, irreversible ChE inhibition by several organophosphate and carbamate compounds was characterized. All the irreversible inhibitions were homogeneous following a second-order rate reaction. The bimolecular rate constant (
k
i
) values of ChE inhibition by the tested pesticides were also estimated and compared with available data from other invertebrate and vertebrate species. In conclusion, the results of the present study showed that prawn eyes possess only one ChE with typical properties of acetylcholinesterase, which is highly sensitive to the tested anti-cholinesterase compounds.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>16497396</pmid><doi>10.1016/j.aquatox.2006.01.011</doi><tpages>10</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Aquatic toxicology, 2006-05, Vol.77 (4), p.412-421 |
| issn | 0166-445X 1879-1514 |
| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Acetylthiocholine - metabolism animal models Animal, plant and microbial ecology Animals Applied ecology Biochemistry, Molecular Biology Biological and medical sciences Biomarker biomarkers carbamate pesticides Carbamates - pharmacokinetics Carbamates - pharmacology Cholinesterase Cholinesterase Inhibitors - pharmacology Cholinesterases - drug effects Cholinesterases - metabolism Ecotoxicology, biological effects of pollution enzyme activation enzyme activity enzyme inhibitors Estuarine invertebrate Eye - drug effects Eye - enzymology eyes Fundamental and applied biological sciences. Psychology General aspects Life Sciences Organophosphate and carbamate pesticides Organophosphates - pharmacokinetics Organophosphates - pharmacology organophosphorus pesticides Palaemon serratus Palaemonidae - drug effects Palaemonidae - enzymology Pesticides - pharmacokinetics Pesticides - pharmacology shrimp Substrate Specificity Thiocholine - analogs & derivatives Thiocholine - metabolism toxicity testing Water Pollutants, Chemical - pharmacokinetics Water Pollutants, Chemical - pharmacology |
| title | Cholinesterase from the common prawn ( Palaemon serratus) eyes: Catalytic properties and sensitivity to organophosphate and carbamate compounds |
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