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Inhibition by Cu 2+ and Cd 2+ of a mu‐class glutathione S‐transferase from shrimp Litopenaeus vannamei
Author(s) -
SalazarMedina Alex J.,
GarcíaRico Leticia,
GarcíaOrozco Karina D.,
ValenzuelaSoto Elisa,
ContrerasVergara Carmen A.,
Arreola Rodrigo,
ArvizuFlores Aldo,
SoteloMundo Rogerio R.
Publication year - 2010
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/jbt.20326
Subject(s) - litopenaeus , glutathione , chemistry , shrimp , cadmium , xenobiotic , glutathione s transferase , enzyme , biochemistry , stereochemistry , microbiology and biotechnology , biology , ecology , organic chemistry
Glutathione S ‐transferases (GSTs) are a family of detoxifying enzymes that catalyze the conjugation of glutathione (GSH) to electrophiles, thereby increasing the solubility of xenobiotics and aiding its excretion from the cell. The present work presents the inhibition of a mu‐class GST of the marine shrimp Litopenaeus vannamei by copper (Cu 2+ ) and cadmium (Cd 2+ ). The protein was overexpressed in bacteria and its enzymatic activity measured using 1‐chloro‐2,4‐dinitrobenzene. The mean inhibitory concentration (IC 50 ) for shrimp GST against Cu 2+ was 4.77 μM and for Cd 2+ was 0.39 μM. A molecular model of the protein based on the crystal structure of a maize GST bound to cadmium showed that the metal binds in the GSH‐binding site by coordination with Asp and Gln residues. These results are consistent with the experimental data and suggest that sublethal concentration of metals may affect the capacity of the organism to detoxify pesticides or xenobiotics. © 2010 Wiley Periodicals, Inc. J Biochem Mol Toxicol 24:218–222, 2010; View this article online at wileyonlinelibrary.com . DOI 10.1002/jbt.20326