PMID:12568595
| Citation |
Hur, S and Bruice, TC (2003) Enzymes do what is expected (chalcone isomerase versus chorismate mutase). J. Am. Chem. Soc. 125:1472-3 |
|---|---|
| Abstract |
Madicago sativa chalcone isomerase (CI) catalyzes the isomerization of chalcone to flavanone, whereas E. coli chorismate mutase (CM) catalyzes the pericyclic rearrangement of chorismate to prephenate. Covalent intermediates are not formed in either of the enzyme-catalyzed reactions, K(M) and k(cat) are virtually the same for both enzymes, and the rate constants (k(o)) for the noncatalyzed reactions in water are also the same. This kinetic identity of both the enzymatic and the nonenzymatic reactions is not shared by a similarity in driving forces. The efficiency (DeltaG(o)() - DeltaG(cat)()) for the CI mechanism involves transition-state stabilization through general-acid catalysis and freeing of three water molecules trapped in the E.S species. The contribution to lowering DeltaG(cat)() by an increase in near attack conformer (NAC) formation in E.S as compared to S in water is not so important. In the CM reaction, the standard free energy for NAC formation in water is 8.4 kcal/mol as compared to 0.6 kcal/mol in E.S. Because the value of (DeltaG(o)() - DeltaG(cat)()) is 9 kcal/mol, the greater percentage of NACs accounts for approximately 90% of the kinetic advantage of the CM reaction. There is no discernible transition-state stabilization in the CM reaction. These results are discussed. In anthropomorphic terms, each enzyme has had to do what it must to have a biologically relevant rate of reaction. |
| Links |
PubMed Online version:10.1021/ja0293047 |
| Keywords |
Catalysis; Chalcone/chemistry; Chalcone/metabolism; Chorismate Mutase/chemistry; Chorismate Mutase/metabolism; Chorismic Acid/chemistry; Chorismic Acid/metabolism; Computer Simulation; Escherichia coli/enzymology; Intramolecular Lyases/chemistry; Intramolecular Lyases/metabolism; Medicago sativa/enzymology; Models, Molecular; Protein Conformation; Thermodynamics |
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