ABSTRACT
Enzymes increase by many orders of magnitude the rates of reactions that would otherwise proceed on glacial timescales. In short, enzymes pick precise target molecules out of the complex cellular milieu and place them in the precise geometry and chemical environment that minimizes the activation energy of the specific desired reaction. Modern transition state theory and computer simulations suggest that the dominant factor in enzymatic catalysis is the lowering of the activation barrier by stabilization of the transition state. C0omputation has emerged as a promising method for taming the complexity of enzyme design. However, the activity of the designed enzyme with ammelide was seven orders of magnitude lower than that of the wild-type enzyme with guanine. In a series of recent breakthrough reports, David Baker and his colleagues have described a novel protocol for the creation of artificial enzymes.
