A unique esterase having a "water-mediated catalytic triad"

Prof. Lammers and Prof. Bornscheuer together with their teams and further collaborators just published an article in Nature Communications (https://doi.org/10.1038/s41467-025-60016-9) dealing with a unique esterase from a marine bacterium. This enzyme contains a novel catalytic triad architecture lacking the typical aspartate for polarization of the histidine. Instead, it contains a precisely coordinated water molecule mediating contact between the His and Asp. This coordinated water in the Ser-His-(H2O-Asp/Asn) motif is crucial for catalytic activity and represents a water-mediated catalytic triad. This joint project was funded by the German Research Foundation within the POMPU project.