ub.xmlui.mirage2.page-structure.muninLogoub.xmlui.mirage2.page-structure.openResearchArchiveLogo
    • EnglishEnglish
    • norsknorsk
  • Velg spraakEnglish 
    • EnglishEnglish
    • norsknorsk
  • Administration/UB
View Item 
  •   Home
  • Fakultet for naturvitenskap og teknologi
  • Institutt for kjemi
  • Artikler, rapporter og annet (kjemi)
  • View Item
  •   Home
  • Fakultet for naturvitenskap og teknologi
  • Institutt for kjemi
  • Artikler, rapporter og annet (kjemi)
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

Evolution of β-lactamases and enzyme promiscuity

Permanent link
https://hdl.handle.net/10037/21539
DOI
https://doi.org/10.1093/protein/gzab013
Thumbnail
View/Open
article.pdf (352.9Kb)
Accepted manuscript version (PDF)
Date
2021-06-08
Type
Journal article
Tidsskriftartikkel
Peer reviewed

Author
Fröhlich, Christopher; Chen, John Z; Gholipour, Sevan; Erdogan, Ayse N; Tokuriki, Nobuhiko
Abstract
β-Lactamases represent one of the most prevalent resistance mechanisms against β-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, β-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 β-lactamases within the two enzyme superfamilies—i.e. the penicillin-binding protein-like and metallo-β-lactamase superfamily—through phylogenetics. We further discuss potential evolutionary origins of each β-lactamase class by highlighting signs of evolutionary connections in protein functions between β-lactamases and other enzymes, especially cases of enzyme promiscuity.
Description
This is a pre-copyedited, author-produced version of an article accepted for publication in Protein Engineering Design & Selection following peer review. The version of record Fröhlich, C.F., Chen, J.Z., Gholipour, S., Erdogan, A.N. & Tokuriki, N. (2021). Evolution of β-lactamases and enzyme promiscuity. Protein Engineering Design & Selection, 34, gzab013, is available online at: https://doi.org/10.1093/protein/gzab013.
Is part of
Fröhlich, C. (2021). On the Evolvability of OXA-48. A comprehensive study of new functions within the β-lactamase OXA-48. (Doctoral thesis). https://hdl.handle.net/10037/21980.
Publisher
Oxford University Press
Citation
Fröhlich, C.F., Chen, J.Z., Gholipour, S., Erdogan, A.N. & Tokuriki, N. (2021). Evolution of β-lactamases and enzyme promiscuity. Protein Engineering Design & Selection, 34, gzab013.
Metadata
Show full item record
Collections
  • Artikler, rapporter og annet (kjemi) [565]
Copyright 2021 The Author(s)

Browse

Browse all of MuninCommunities & CollectionsAuthor listTitlesBy Issue DateBrowse this CollectionAuthor listTitlesBy Issue Date
Login

Statistics

View Usage Statistics
UiT

Munin is powered by DSpace

UiT The Arctic University of Norway
The University Library
uit.no/ub - munin@ub.uit.no

Accessibility statement (Norwegian only)