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Serine proteases: how did chemists tease out their catalytic mechanism?

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Serine proteases are a family of enzymes that degrade a wide range of proteins and play vital roles in a variety of biological processes. Their mechanism of action involves several catalytic strategies that are common in enzymatic catalysis. In this article, we review the catalytic mechanism of serine proteases and how it was elucidated over the years. The artful application of chemical probes to dissect the mechanism of serine proteases provides excellent examples for teaching present-day students and scientists how to solve complex chemical and biological problems through chemical logic.

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Adapted with permission from [4]. Copyright 2002, American Chemical Society

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Adapted with permission from [25]. Copyright 1976, American Chemical Society

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Acknowledgements

V. Blay thanks the Ohio State University, Fisher College of Business for support. The article is based on selected content from the course “Enzymes” (BIOCHEM 6762, Ohio State University), created by Prof. Dehua Pei and Prof. Ming-Daw Tsai.

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Authors and Affiliations

  1. Department of Chemistry and Biochemistry, The Ohio State University, 100 West 18th Avenue, Columbus, OH, 43210, USA

    Vincent Blay & Dehua Pei

  2. Department of Microbiology and Environmental Toxicology, University of California, Santa Cruz, Santa Cruz, CA, 95064, USA

    Vincent Blay

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  1. Vincent Blay
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  2. Dehua Pei
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Correspondence to Vincent Blay.

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Blay, V., Pei, D. Serine proteases: how did chemists tease out their catalytic mechanism?. ChemTexts 5, 19 (2019). https://doi.org/10.1007/s40828-019-0093-4

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