{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["294(30)"],"submitter":["Newcomer ME"],"pubmed_abstract":["On the fiftieth anniversary of the discovery of the Ser-His-Asp catalytic triad, perhaps the most unusual variation on the textbook classic is described: An incomplete catalytic triad in a hydrolase is rescued by a chloride ion (Fig. 1). Structural and functional data provide compelling evidence that the active site of a phospholipase from <i>Vibrio vulnificus</i> employs the anion in place of the commonly observed Asp, reminding us that even well-trodden scientific ground has surprises in store."],"journal":["The Journal of biological chemistry"],"pagination":["11402-11403"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6663875"],"repository":["biostudies-literature"],"pubmed_title":["Chloride to the rescue."],"pmcid":["PMC6663875"],"pubmed_authors":["Newcomer ME"],"additional_accession":[]},"is_claimable":false,"name":"Chloride to the rescue.","description":"On the fiftieth anniversary of the discovery of the Ser-His-Asp catalytic triad, perhaps the most unusual variation on the textbook classic is described: An incomplete catalytic triad in a hydrolase is rescued by a chloride ion (Fig. 1). Structural and functional data provide compelling evidence that the active site of a phospholipase from <i>Vibrio vulnificus</i> employs the anion in place of the commonly observed Asp, reminding us that even well-trodden scientific ground has surprises in store.","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Jul","modification":"2025-05-31T23:55:49.98Z","creation":"2025-05-31T23:55:49.98Z"},"accession":"S-EPMC6663875","cross_references":{"pubmed":["31350284"],"doi":["10.1074/jbc.H119.009687","10.1074/jbc.h119.009687"]}}