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

Evolution of β-lactamases and enzyme promiscuity

Permanent lenke
https://hdl.handle.net/10037/21539
DOI
https://doi.org/10.1093/protein/gzab013
Thumbnail
Åpne
article.pdf (352.9Kb)
Akseptert manusversjon (PDF)
Dato
2021-06-08
Type
Journal article
Tidsskriftartikkel
Peer reviewed

Forfatter
Fröhlich, Christopher; Chen, John Z; Gholipour, Sevan; Erdogan, Ayse N; Tokuriki, Nobuhiko
Sammendrag
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.
Beskrivelse
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.
Er en del av
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.
Forlag
Oxford University Press
Sitering
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
Vis full innførsel
Samlinger
  • Artikler, rapporter og annet (kjemi) [565]
Copyright 2021 The Author(s)

Bla

Bla i hele MuninEnheter og samlingerForfatterlisteTittelDatoBla i denne samlingenForfatterlisteTittelDato
Logg inn

Statistikk

Antall visninger
UiT

Munin bygger på DSpace

UiT Norges Arktiske Universitet
Universitetsbiblioteket
uit.no/ub - munin@ub.uit.no

Tilgjengelighetserklæring