Abstract
This Special Issue comprises twelve authoritative reviews that highlight an understudied but rapidly developing area of biology: catalytically inactive enzyme homologs. These pseudoenzymes, sometimes called ‘dead enzymes’, are found within most enzyme families and generally arose via gene duplication events. Dead enzymes have lost their enzymatic capacity, often via the evolutionary loss of key catalytic residues. However, as this Special Issue highlights, pseudoenzymes are far from being functionally ‘dead’. In fact, they fulfill a range of critical biochemical roles, frequently appearing more versatile as biochemical regulators than their catalytic cousins. The functions of dead enzymes from diverse enzyme families often follow recurring themes, including allosteric regulation of their catalytically active counterparts, acting as signaling scaffolds, or as inhibitors that recognize and sequester the substrates of their catalytic homologs. As well as highlighting the breadth and depth of dead enzyme biology, this Special Issue emphasizes the power of pseudoenzymes as key biochemical regulators in health and disease and potentially as more tractable drug targets than some enzymes themselves. We hope you find these reviews enlivening, and we thank the authors for these excellent contributions.
Original language | English |
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Pages (from-to) | 4102-4105 |
Number of pages | 4 |
Journal | FEBS journal |
Volume | 287 |
Issue number | 19 |
DOIs | |
Publication status | Published - 07 Oct 2020 |
Bibliographical note
Funding Information:I thank colleagues for helpful discussions and inspiration at the EMBO workshop entitled ?Pseudoenzymes: From molecular mechanisms to cell biology? held in Cagliari, Italy, in May 2018. I thank Matthew Freeman, who introduced me to the world of ?dead enzymes?, and Pat Eyers, a key ?scaffold? who nucleates the pseudoenzyme community. We are grateful for the ongoing support of our laboratory by Funda??o Calouste Gulbenkian, Queen?s University Belfast, Funda??o para a Ci?ncia e Tecnologia (project LISBOA-01-0145-FEDER-031330) and ?La Caixa? Foundation (ID 100010434), under the agreement <LCF/PR/HR17/52150018>.
Funding Information:
We are grateful for the ongoing support of our laboratory by Fundação Calouste Gulbenkian, Queen’s University Belfast, Fundação para a Ciência e Tecnologia (project LISBOA‐01‐0145‐FEDER‐031330) and ‘La Caixa’ Foundation (ID 100010434), under the agreement .
Publisher Copyright:
© 2020 Federation of European Biochemical Societies
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology