The reaction mechanism of LipA hydrolyzing the (R)-Roche ester and a model reaction coordinate for the active site theozyme.

The reaction mechanism of LipA hydrolyzing the (R)-Roche ester and a model reaction coordinate for the active site theozyme.

<p><i>∆G values shown in the reaction coordinate are for a “linear” substrate conformation, where the tail hydroxyl group does</i><i>not hydrogen bond with the carbonyl oxygen or the ester oxygen.</i></p>

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Bibliographic Details
Main Author:	Spencer Gardiner (22238328) (author)
Other Authors:	Peter Dollinger (12635588) (author), Filip Kovacic (125554) (author), Jörg Pietruszka (3027846) (author), Daniel H. Ess (1323651) (author), Karl-Erich Jaeger (125594) (author), Gunnar F. Schröder (22238331) (author), Dennis Della Corte (8736135) (author)
Published:	2025
Subjects:	Biophysics Biochemistry Biotechnology Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified Information Systems not elsewhere classified small energetic shifts sensitive ranking metrics reactive force fields pseudomonas aeruginosa </ post hoc </ point mutations based hydrogen bond formation density functional theory based energy scoring using design tools like activity improvements incremental activity changes deep learning models deep learning methods div >< p deep learning effects using targeting non substrate conformation substrate binding structural proximity structural prediction results highlight residue flexibility optimizing biocatalysts natural substrates mol depending likely critical initial set improved benchmarks existing approaches designing enzymes current computational case study active site
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