Abstract
A wide variety of peptidases associate with vital biological pathways, but the origin and evolution of their tremendous diversity are poorly defined. Application of the MEROPS classification to a comprehensive set of genomes yields a simple pattern of peptidase distribution and provides insight into the organization of proteolysis in all forms of life. Unexpectedly, a near ubiquitous core set of peptidases is shown to contain more types than those unique to higher multicellular organisms. From this core group, an array of eukaryote-specific peptidases evolved to yield well known intracellular and extracellular processes. The paucity of peptidase families unique to higher metazoa suggests gains in proteolytic network complexity required a limited number of biochemical inventions. These findings provide a framework for deeper investigation into the evolutionary forces that shaped each peptidase family and a roadmap to develop a time-line for their expansion as an interconnected system. © 2008 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Page, M. J., & Di Cera, E. (2008). Evolution of peptidase diversity. Journal of Biological Chemistry, 283(44), 30010–30014. https://doi.org/10.1074/jbc.M804650200
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