Enzyme promiscuity shapes adaptation to novel growth substrates.
adaptive evolution
enzyme promiscuity
genome‐scale modeling
systems biology
Journal
Molecular systems biology
ISSN: 1744-4292
Titre abrégé: Mol Syst Biol
Pays: England
ID NLM: 101235389
Informations de publication
Date de publication:
08 04 2019
08 04 2019
Historique:
entrez:
10
4
2019
pubmed:
10
4
2019
medline:
1
5
2020
Statut:
epublish
Résumé
Evidence suggests that novel enzyme functions evolved from low-level promiscuous activities in ancestral enzymes. Yet, the evolutionary dynamics and physiological mechanisms of how such side activities contribute to systems-level adaptations are not well characterized. Furthermore, it remains untested whether knowledge of an organism's promiscuous reaction set, or underground metabolism, can aid in forecasting the genetic basis of metabolic adaptations. Here, we employ a computational model of underground metabolism and laboratory evolution experiments to examine the role of enzyme promiscuity in the acquisition and optimization of growth on predicted non-native substrates in
Identifiants
pubmed: 30962359
doi: 10.15252/msb.20188462
pmc: PMC6452873
doi:
Substances chimiques
Enzymes
0
Escherichia coli Proteins
0
Succinates
0
Tartrates
0
Deoxyribose
533-67-5
Arabinose
B40ROO395Z
tartaric acid
W4888I119H
monomethyl succinate
YA2V724S0A
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
e8462Subventions
Organisme : Wellcome Trust
Pays : United Kingdom
Informations de copyright
© 2019 The Authors. Published under the terms of the CC BY 4.0 license.
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