Dynamic model for enzyme action.
BACKGROUND
Protein thermodynamic structure theory is an integrated approach to the study of protein dynamics and the mechanisms of enzyme catalysis. In this paper, a hypothesis arising from this theory is examined. The timescale of an enzymatic reaction (TER) gives a key to characterizing enzyme conformational changes. The aspects of timescale important in our approach are: (i) it is logically related to internal motions of the main chain of a protein; (ii) it sets the upper limit on the size or scope of protein conformational changes. Feature (i) is linked to the dynamic properties of enzyme-reactant complexes. Feature (ii) is linked to the dynamic sites of the main chain (promoting motion) involved in enzyme activity.


CONCLUSIONS
Our analysis shows that a comprehensive understanding of enzymology can be established on the basis of protein thermodynamic structure theory.
Department of Biochemistry and Molecular Biology, Medical Institute, P. O. Box 2619, Beijing 100068, PR China.
Qinyi
Q
Zhao
D000494:Allosteric Regulation; D002384:Catalysis; D004798:Enzymes; D007700:Kinetics; D008954:Models, Biological; D011485:Protein Binding; D011487:Protein Conformation; D013816:Thermodynamics
D004798:Enzymes