biostudies-literatureVazquez-Armenta FJConsejo Nacional de Ciencia y TecnologíaNational Autonomous University of MexicoUniversidad de Sonora609https://www.ebi.ac.uk/biostudies/studies/S-EPMC9506434biostudies-literatureUnknown14(9)Lecithin-dependent thermolabile hemolysin (LDH) is a virulence factor excreted by Vibrio parahaemolyticus, a marine bacterium that causes important losses in shrimp farming. In this study, the function of LDH was investigated through its inhibition by metal ions (Mg2+, Ca2+, Mn2+, Co2+, Ni2+ and Cu2+) and chemical modification reagents: β-mercaptoethanol (βME), phenylmethylsulfonyl fluoride (PMSF) and diethyl pyrocarbonate (DEPC). LDH was expressed in the Escherichia coli strain BL-21, purified under denaturing conditions, and the enzymatic activity was evaluated. Cu2+, Ni2+, Co2+ and Ca2+ at 1 mmol/L inhibited the LDH esterase activity by 20−95%, while Mg2+ and Mn2+ slightly increased its activity. Additionally, PMSF and DEPC at 1 mmol/L inhibited the enzymatic activity by 40% and 80%, reToxinsMetal Ions and Chemical Modification Reagents Inhibit the Enzymatic Activity of Lecithin-Dependent Hemolysin from <i>Vibrio parahaemolyticus</i>.PMC9506434UNISON-DCBS-2022-USO313007854Ciencia-Frontera-2019-263986UNAM-CIC-UNISON-2018 and − 2019Ayala-Zavala JFVazquez-Armenta FJValdez-Olmos UFLopez-Zavala AAOchoa-Leyva AArvizu-Flores AAfalseMetal Ions and Chemical Modification Reagents Inhibit the Enzymatic Activity of Lecithin-Dependent Hemolysin from <i>Vibrio parahaemolyticus</i>.Lecithin-dependent thermolabile hemolysin (LDH) is a virulence factor excreted by Vibrio parahaemolyticus, a marine bacterium that causes important losses in shrimp farming. In this study, the function of LDH was investigated through its inhibition by metal ions (Mg2+, Ca2+, Mn2+, Co2+, Ni2+ and Cu2+) and chemical modification reagents: β-mercaptoethanol (βME), phenylmethylsulfonyl fluoride (PMSF) and diethyl pyrocarbonate (DEPC). LDH was expressed in the Escherichia coli strain BL-21, purified under denaturing conditions, and the enzymatic activity was evaluated. Cu2+, Ni2+, Co2+ and Ca2+ at 1 mmol/L inhibited the LDH esterase activity by 20−95%, while Mg2+ and Mn2+ slightly increased its activity. Additionally, PMSF and DEPC at 1 mmol/L inhibited the enzymatic activity by 40% and 80%, re2022-01-01T00:00:00Z2022 Sep2025-05-31T23:13:31.115Z2024-11-12T02:34:07.32ZS-EPMC95064343613654710.3390/toxins14090609