Introduction to the Thematic Minireview Series: Radical SAM Enzymes [Enzymology]

December 4th, 2014 by Banerjee, R.

In the early days, radical enzyme reactions that use S-adenosylmethionine (SAM) coordinated to an Fe-S cluster, which Perry Frey described as a "poor man's coenzyme B12", were believed to be relatively rare chemical curiosities. Today, bioinformatics analyses have revealed the wide prevalence and sheer numbers of radical SAM enzymes, conferring superfamily status. In this thematic minireview series, the JBC presents six articles on radical SAM enzymes that accomplish wide-ranging chemical transformations. We learn that despite the diversity of the reactions catalyzed, family members share some common structural and mechanistic themes. Still in its infancy, continued explorations promise to be fertile grounds for discoveries that will undoubtedly further broaden our understanding of the catalytic repertoire and deepen our understanding of the chemical strategies used by radical SAM enzymes.

Introduction to the Thematic Minireview Series Enzyme Evolution [Protein Structure and Folding]

September 10th, 2014 by Banerjee, R.

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.