biostudies-literatureUnknown294(30)Newcomer MEOn 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.The Journal of biological chemistry11402-11403https://www.ebi.ac.uk/biostudies/studies/S-EPMC6663875biostudies-literatureChloride to the rescue.PMC6663875Newcomer MEfalseChloride to the rescue.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.2019-01-01T00:00:00Z2019 Jul2025-05-31T23:55:49.98Z2025-05-31T23:55:49.98ZS-EPMC66638753135028410.1074/jbc.H119.00968710.1074/jbc.h119.009687