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Cooperativity and flexibility in enzyme evolution

Pabis, Anna ; Risso, Valeria A ; Sanchez-Ruiz, Jose M and Kamerlin, Shina Cl LU orcid (2018) In Current Opinion in Structural Biology 48. p.83-92
Abstract

Enzymes are flexible catalysts, and there has been substantial discussion about the extent to which this flexibility contributes to their catalytic efficiency. What has been significantly less discussed is the extent to which this flexibility contributes to their evolvability. Despite this, recent years have seen an increasing number of both experimental and computational studies that demonstrate that cooperativity and flexibility play significant roles in enzyme innovation. This review covers key developments in the field that emphasize the importance of enzyme dynamics not just to the evolution of new enzyme function(s), but also as a property that can be harnessed in the design of new artificial enzymes.

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author
; ; and
publishing date
type
Contribution to journal
publication status
published
keywords
Amino Acid Motifs, Animals, Aryldialkylphosphatase/chemistry, Bacteria/classification, Biocatalysis, Catalytic Domain, Evolution, Molecular, Humans, Models, Molecular, Phosphoric Monoester Hydrolases/chemistry, Phylogeny, Protein Conformation, Structure-Activity Relationship, Substrate Specificity, Tetrahydrofolate Dehydrogenase/chemistry, beta-Lactamases/chemistry
in
Current Opinion in Structural Biology
volume
48
pages
10 pages
publisher
Elsevier
external identifiers
  • pmid:29141202
  • scopus:85034018445
ISSN
1879-033X
DOI
10.1016/j.sbi.2017.10.020
language
English
LU publication?
no
additional info
Copyright © 2017 The Authors. Published by Elsevier Ltd.. All rights reserved.
id
e7af1d9f-2b99-4c2c-9f31-3f80b1b2b62e
date added to LUP
2025-01-11 21:20:17
date last changed
2025-07-13 18:46:18
@article{e7af1d9f-2b99-4c2c-9f31-3f80b1b2b62e,
  abstract     = {{<p>Enzymes are flexible catalysts, and there has been substantial discussion about the extent to which this flexibility contributes to their catalytic efficiency. What has been significantly less discussed is the extent to which this flexibility contributes to their evolvability. Despite this, recent years have seen an increasing number of both experimental and computational studies that demonstrate that cooperativity and flexibility play significant roles in enzyme innovation. This review covers key developments in the field that emphasize the importance of enzyme dynamics not just to the evolution of new enzyme function(s), but also as a property that can be harnessed in the design of new artificial enzymes.</p>}},
  author       = {{Pabis, Anna and Risso, Valeria A and Sanchez-Ruiz, Jose M and Kamerlin, Shina Cl}},
  issn         = {{1879-033X}},
  keywords     = {{Amino Acid Motifs; Animals; Aryldialkylphosphatase/chemistry; Bacteria/classification; Biocatalysis; Catalytic Domain; Evolution, Molecular; Humans; Models, Molecular; Phosphoric Monoester Hydrolases/chemistry; Phylogeny; Protein Conformation; Structure-Activity Relationship; Substrate Specificity; Tetrahydrofolate Dehydrogenase/chemistry; beta-Lactamases/chemistry}},
  language     = {{eng}},
  pages        = {{83--92}},
  publisher    = {{Elsevier}},
  series       = {{Current Opinion in Structural Biology}},
  title        = {{Cooperativity and flexibility in enzyme evolution}},
  url          = {{http://dx.doi.org/10.1016/j.sbi.2017.10.020}},
  doi          = {{10.1016/j.sbi.2017.10.020}},
  volume       = {{48}},
  year         = {{2018}},
}