Abstract
The results of crystallographic analysis of a complex between an aspartic proteinase, endothiapepsin, and an inhibitor have been extended through the assignment of protons in the active site, to study various steps in the reaction with a substrate. Mechanistic implications are suggested as a consequence of semiempirical quantum mechanical calculations, indicating that most of the activation energy is required to bring the substrate from an initial binding mode to close distance to a water molecule.
Original language | American English |
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Pages (from-to) | 270-274 |
Number of pages | 5 |
Journal | Journal of Chemical Information and Computer Sciences |
Volume | 33 |
Issue number | 2 |
DOIs | |
State | Published - 1993 |