THERMODYNAMIC TRAJECTORY OF ENZYME EVOLUTION

Authors
Citation
M. Kodaka et A. Hase, THERMODYNAMIC TRAJECTORY OF ENZYME EVOLUTION, Journal of physical chemistry, 99(26), 1995, pp. 10686-10689
Citations number
5
Categorie Soggetti
Chemistry Physical
ISSN journal
00223654
Volume
99
Issue
26
Year of publication
1995
Pages
10686 - 10689
Database
ISI
SICI code
0022-3654(1995)99:26<10686:TTOEE>2.0.ZU;2-R
Abstract
The trajectory of enzyme evolution is estimated from the relationship between the overall enthalpy of activation and overall entropy of acti vation. As evolution proceeds, the trajectory passes a turning point a nd then go toward diffusion-controlled region. Thus, the following two possibilities are put forth as candidates of a goal of evolution. One is that evolution will stop at a turning point, where specificity of a reaction is highest. The other is that the ultimate goal of evolutio n is the diffusion-controlled reaction, where catalytic efficiency is highest.