A meta-analysis of the activity, stability, and mutational characteristics of temperature-adapted enzymes.
enzyme activity
enzymology
extremophiles
mutation
protein stability
Journal
Bioscience reports
ISSN: 1573-4935
Titre abrégé: Biosci Rep
Pays: England
ID NLM: 8102797
Informations de publication
Date de publication:
30 04 2021
30 04 2021
Historique:
received:
04
02
2021
revised:
29
03
2021
accepted:
19
04
2021
pubmed:
20
4
2021
medline:
24
12
2021
entrez:
19
4
2021
Statut:
ppublish
Résumé
Understanding the characteristics that define temperature-adapted enzymes has been a major goal of extremophile enzymology in recent decades. In the present study, we explore these characteristics by comparing psychrophilic, mesophilic, and thermophilic enzymes. Through a meta-analysis of existing data, we show that psychrophilic enzymes exhibit a significantly larger gap (Tg) between their optimum and melting temperatures compared with mesophilic and thermophilic enzymes. These results suggest that Tg may be a useful indicator as to whether an enzyme is psychrophilic or not and that models of psychrophilic enzyme catalysis need to account for this gap. Additionally, by using predictive protein stability software, HoTMuSiC and PoPMuSiC, we show that the deleterious nature of amino acid substitutions to protein stability increases from psychrophiles to thermophiles. How this ultimately affects the mutational tolerance and evolutionary rate of temperature adapted organisms is currently unknown.
Identifiants
pubmed: 33871022
pii: 228416
doi: 10.1042/BSR20210336
pmc: PMC8150157
pii:
doi:
Types de publication
Journal Article
Meta-Analysis
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© 2021 The Author(s).
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