Abstract
Experimental analysis of enzymatic transition states by kinetic isotope effect methods has established geometric variation in related transition state structures. Differences are apparent in development of the reaction coordinate, in solvolytic transition states relative to those in enzymatic catalytic sites, in the stereochemistry of related substrates at the transition state, and in reactions catalyzed by related enzymes.
Original language | English (US) |
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Pages (from-to) | 556-564 |
Number of pages | 9 |
Journal | Current Opinion in Chemical Biology |
Volume | 5 |
Issue number | 5 |
DOIs | |
State | Published - Oct 1 2001 |
ASJC Scopus subject areas
- Analytical Chemistry
- Biochemistry