Journal
PROTEIN SCIENCE
Volume 17, Issue 12, Pages 2023-2037Publisher
WILEY
DOI: 10.1110/ps.035436.108
Keywords
enzymes; active sites; structure/function studies; protein turnover; structure; serine proteases; threonine proteases
Categories
Funding
- National Sciences Foundation [MCB-0316670]
- Canadian Institute of Health
- National Science and Engineering
- Michael Smith Foundation
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Serine proteases comprise nearly one-third of all known proteases identified to date and play crucial roles in a wide variety of cellular as well as extracellular functions, including the process of blood clotting, protein digestion, cell signaling, inflammation, and protein processing. Their hallmark is that they contain the so-called classical'' catalytic Ser/His/Asp triad. Although the classical serine proteases are the most widespread in nature, there exist a variety of nonclassical'' serine proteases where variations to the catalytic triad are observed. Such variations include the triads Ser/His/Glu, Ser/His/His, and Ser/Glu/Asp, and include the dyads Ser/Lys and Ser/His. Other variations are seen with certain serine and threonine peptidases of the Ntn hydrolase superfamily that carry out catalysis with a single active site residue. This work discusses the structure and function of these novel serine proteases and threonine proteases and how their catalytic machinery differs from the prototypic serine protease class.
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