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 (Cu2+) and cadmium (Cd2+). The protein was overexpressed in bacteria and its enzymatic activity measured using 1-chloro-2,4-dinitrobenzene. The mean inhibitory concentration (IC50) for shrimp GST against Cu2+ was 4.77 μM and for Cd2+ 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