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Enzymatic transition states and transition state analog design
1Department of Biochemistry, Albert Einstein College of Medicine of Yeshiva University, Bronx, New York 10461, USA. vern@aecom.yu.edu
Annual Review of Biochemistry
|October 6, 1998
Summary
Enzymes catalyze reactions by stabilizing unstable transition states. Understanding enzyme transition state structure aids in designing effective inhibitors and provides insights into catalytic mechanisms.
Area of Science:
- Biochemistry
- Chemical Kinetics
Background:
- Enzymes accelerate biochemical reactions by lowering activation energy.
- Enzymatic catalysis is understood through the stabilization of unstable transition states.
- Direct observation of enzyme-bound transition states is challenging.
Purpose of the Study:
- To review transition state theory for enzymatic reactions.
- To compare enzymatic and chemical transition states.
- To explore the design of transition state inhibitors.
Main Methods:
- Analysis of kinetic isotope effects.
- Computational chemistry.
- Comparison of transition state inhibitors with enzymatic transition states.
Main Results:
- Kinetic isotope effects provide geometric and electronic structure of enzyme-bound transition states.
- Transition state structure information aids in comparing chemical and enzymatic reactions.
- Enzymatic activators' effects on transition state structure can be determined.
Conclusions:
- Enzymatic transition state structure is central to understanding enzyme catalysis.
- Knowledge of transition states enables the design of potent enzyme inhibitors.
- This approach deepens the understanding of enzyme mechanisms and inhibitor design.
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