期刊
PROTEIN ENGINEERING DESIGN & SELECTION
卷 34, 期 -, 页码 -出版社
OXFORD UNIV PRESS
DOI: 10.1093/protein/gzab013
关键词
beta-lactamase; enzyme promiscuity; evolution; promiscuous activity
资金
- Canadian Institute of Health Research (CIHR) Foundation [FDN-148437]
- Norwegian PhD School of Pharmacy
- National Graduate School in Infection Biology and Antimicrobials
- National Graduate School in Biocatalysis
Beta-lactamases are a common resistance mechanism against beta-lactam antibiotics and have become important models in enzymology and evolutionary biochemistry. They have evolved multiple times from distinct evolutionary origins, exhibiting diverse structural features and enzymatic mechanisms. Understanding their evolution and diversity can aid various disciplines.
beta-Lactamases represent one of the most prevalent resistance mechanisms against beta-lactam antibiotics. Beyond their clinical importance, they have also become key models in enzymology and evolutionary biochemistry. A global understanding of their evolution and sequence and functional diversity can therefore aid a wide set of different disciplines. Interestingly, beta-lactamases have evolved multiple times from distinct evolutionary origins, with ancestries that reach back billions of years. It is therefore no surprise that these enzymes exhibit diverse structural features and enzymatic mechanisms. In this review, we provide a bird's eye view on the evolution of beta-lactamases within the two enzyme superfamilies-i.e. the penicillin-binding protein-like and metallo-beta-lactamase superfamily-through phylogenetics. We further discuss potential evolutionary origins of each beta-lactamase class by highlighting signs of evolutionary connections in protein functions between beta-lactamases and other enzymes, especially cases of enzyme promiscuity.
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