Temperature as a modulator of allosteric motions and crosstalk in mesophilic and thermophilic enzymes

Mesophilic and thermophilic enzyme counterparts are often studied to understand how proteins function under harsh conditions. To function well outside of standard temperature ranges, thermophiles often tightly regulate their structural ensemble through intra-protein communication (via allostery) and...

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Main Authors: Alexa L. Knight, Vinnie Widjaja, George P. Lisi
Format: Article
Language:English
Published: Frontiers Media S.A. 2023-10-01
Series:Frontiers in Molecular Biosciences
Subjects:
Online Access:https://www.frontiersin.org/articles/10.3389/fmolb.2023.1281062/full
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author Alexa L. Knight
Vinnie Widjaja
George P. Lisi
author_facet Alexa L. Knight
Vinnie Widjaja
George P. Lisi
author_sort Alexa L. Knight
collection DOAJ
description Mesophilic and thermophilic enzyme counterparts are often studied to understand how proteins function under harsh conditions. To function well outside of standard temperature ranges, thermophiles often tightly regulate their structural ensemble through intra-protein communication (via allostery) and altered interactions with ligands. It has also become apparent in recent years that the enhancement or diminution of allosteric crosstalk can be temperature-dependent and distinguish thermophilic enzymes from their mesophilic paralogs. Since most studies of allostery utilize chemical modifications from pH, mutations, or ligands, the impact of temperature on allosteric function is comparatively understudied. Here, we discuss the biophysical methods, as well as critical case studies, that dissect temperature-dependent function of mesophilic-thermophilic enzyme pairs and their allosteric regulation across a range of temperatures.
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spelling doaj.art-0384456f4c4841719588498e970f4c092023-10-09T10:28:56ZengFrontiers Media S.A.Frontiers in Molecular Biosciences2296-889X2023-10-011010.3389/fmolb.2023.12810621281062Temperature as a modulator of allosteric motions and crosstalk in mesophilic and thermophilic enzymesAlexa L. KnightVinnie WidjajaGeorge P. LisiMesophilic and thermophilic enzyme counterparts are often studied to understand how proteins function under harsh conditions. To function well outside of standard temperature ranges, thermophiles often tightly regulate their structural ensemble through intra-protein communication (via allostery) and altered interactions with ligands. It has also become apparent in recent years that the enhancement or diminution of allosteric crosstalk can be temperature-dependent and distinguish thermophilic enzymes from their mesophilic paralogs. Since most studies of allostery utilize chemical modifications from pH, mutations, or ligands, the impact of temperature on allosteric function is comparatively understudied. Here, we discuss the biophysical methods, as well as critical case studies, that dissect temperature-dependent function of mesophilic-thermophilic enzyme pairs and their allosteric regulation across a range of temperatures.https://www.frontiersin.org/articles/10.3389/fmolb.2023.1281062/fullNMRthermodynamicskineticstemperatureallosterythermophiles
spellingShingle Alexa L. Knight
Vinnie Widjaja
George P. Lisi
Temperature as a modulator of allosteric motions and crosstalk in mesophilic and thermophilic enzymes
Frontiers in Molecular Biosciences
NMR
thermodynamics
kinetics
temperature
allostery
thermophiles
title Temperature as a modulator of allosteric motions and crosstalk in mesophilic and thermophilic enzymes
title_full Temperature as a modulator of allosteric motions and crosstalk in mesophilic and thermophilic enzymes
title_fullStr Temperature as a modulator of allosteric motions and crosstalk in mesophilic and thermophilic enzymes
title_full_unstemmed Temperature as a modulator of allosteric motions and crosstalk in mesophilic and thermophilic enzymes
title_short Temperature as a modulator of allosteric motions and crosstalk in mesophilic and thermophilic enzymes
title_sort temperature as a modulator of allosteric motions and crosstalk in mesophilic and thermophilic enzymes
topic NMR
thermodynamics
kinetics
temperature
allostery
thermophiles
url https://www.frontiersin.org/articles/10.3389/fmolb.2023.1281062/full
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