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Cholinesterase from the common prawn (Palaemon serratus) eyes: catalytic properties and sensitivity to organophosphate and carbamate compounds
Frasco, M.F.; Fournier, D.; Carvalho, F.; Guilhermino, L. (2006). Cholinesterase from the common prawn (Palaemon serratus) eyes: catalytic properties and sensitivity to organophosphate and carbamate compounds. Aquat. Toxicol. 77(4): 412-421. dx.doi.org/10.1016/j.aquatox.2006.01.011
In: Aquatic Toxicology. Elsevier Science: Tokyo; New York; London; Amsterdam. ISSN 0166-445X; e-ISSN 1879-1514, more
Peer reviewed article  
Available in  Authors 
Keywords
    Agents > Inhibitors > Enzyme inhibitors > Cholinesterase inhibitors
    Aquatic organisms > Marine organisms > Aquatic animals > Marine invertebrates
    Biomarkers
    Pesticides > Carbamate pesticides
    Water bodies > Coastal waters > Coastal landforms > Coastal inlets > Estuaries
    Palaemon serratus (Pennant, 1777) [WoRMS]
    Marine/Coastal; Brackish water
Authors  Top 
  • Frasco, M.F.
  • Fournier, D.
  • Carvalho, F.
  • Guilhermino, L.
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 (ki) 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.
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