{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Vazquez-Armenta FJ"],"funding":["Consejo Nacional de Ciencia y Tecnología","National Autonomous University of Mexico","Universidad de Sonora"],"pagination":["609"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9506434"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(9)"],"pubmed_abstract":["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%, re"],"journal":["Toxins"],"pubmed_title":["Metal Ions and Chemical Modification Reagents Inhibit the Enzymatic Activity of Lecithin-Dependent Hemolysin from <i>Vibrio parahaemolyticus</i>."],"pmcid":["PMC9506434"],"funding_grant_id":["UNISON-DCBS-2022-USO313007854","Ciencia-Frontera-2019-263986","UNAM-CIC-UNISON-2018 and − 2019"],"pubmed_authors":["Ayala-Zavala JF","Vazquez-Armenta FJ","Valdez-Olmos UF","Lopez-Zavala AA","Ochoa-Leyva A","Arvizu-Flores AA"],"additional_accession":[]},"is_claimable":false,"name":"Metal Ions and Chemical Modification Reagents Inhibit the Enzymatic Activity of Lecithin-Dependent Hemolysin from <i>Vibrio parahaemolyticus</i>.","description":"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%, re","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Sep","modification":"2025-05-31T23:13:31.115Z","creation":"2024-11-12T02:34:07.32Z"},"accession":"S-EPMC9506434","cross_references":{"pubmed":["36136547"],"doi":["10.3390/toxins14090609"]}}