Enzymes are the principal catalysts in biology and comprise a large propor- tion of the proteins encoded by the human genome. Although much has been learned about enzymes over the past century, there are still major gaps in our fundamental knowledge about how enzymes catalyze reactions, what specific substrates are processed by particular enzymes, how enzymes are turned off or on in cellular pathways, and how they influence health and disease. There are increasing numbers of therapeutics that work as enzyme inhibitors and structure-based design is becoming an important part of the arsenal of drug discovery efforts. New technologies involving chemical, biophysical, genetic, and physiologic approaches are changing the landscape of enzyme research and leading to impactful discoveries in enzymology. This issue of COSTBI includes a series of articles that summarize recent advances in the enzyme sciences.

Editorial overview: Biological catalysis at the cross-roads of signaling and metabolism

Mattevi A.
Conceptualization
2019-01-01

Abstract

Enzymes are the principal catalysts in biology and comprise a large propor- tion of the proteins encoded by the human genome. Although much has been learned about enzymes over the past century, there are still major gaps in our fundamental knowledge about how enzymes catalyze reactions, what specific substrates are processed by particular enzymes, how enzymes are turned off or on in cellular pathways, and how they influence health and disease. There are increasing numbers of therapeutics that work as enzyme inhibitors and structure-based design is becoming an important part of the arsenal of drug discovery efforts. New technologies involving chemical, biophysical, genetic, and physiologic approaches are changing the landscape of enzyme research and leading to impactful discoveries in enzymology. This issue of COSTBI includes a series of articles that summarize recent advances in the enzyme sciences.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11571/1300706
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