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Updated: Apr 24, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
Introduction to the thematic minireview series on enzyme evolution
1Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109-0600.
Abstract:
In this thematic minireview series, the JBC presents five provocative articles on Enzyme Evolution. The reviews discuss stimulating concepts that include the emergence of primordial catalysts at temperatures that were considerably warmer than present day ones and the impact of the cooling environment on the evolution of catalytic fitness and the preservation of catalysis-promoting conformational dynamics. They also discuss the use of Urzymes or invariant modules in enzyme superfamilies as paradigms for understanding the evolution of catalytic efficiency and specificity, the use of bioinformatics approaches to understand the roles of substrate ambiguity and catalytic promiscuity as drivers of evolution, and the challenges associated with assigning catalytic function as the number of superfamily members grows rapidly.
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