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Chemical Mapping Ex...
Chemical Mapping Exposes the Importance of Active Site Interactions in Governing the Temperature Dependence of Enzyme Turnover
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- Winter, S. D. (författare)
- Univ Bath, Dept Biol & Biochem, Bath BA2 7AY, Avon, England.
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- Jones, H. B. L. (författare)
- Univ Bath, Dept Biol & Biochem, Bath BA2 7AY, Avon, England.
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- Răsădean, D. M. (författare)
- Univ Bath, Dept Chem, Bath BA2 7AY, Avon, England.
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- Crean, Rory M. (författare)
- Uppsala universitet,Biokemi,Science for Life Laboratory, SciLifeLab
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- Danson, M. J. (författare)
- Univ Bath, Dept Biol & Biochem, Bath BA2 7AY, Avon, England.
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- Pantoş, G. D. (författare)
- Univ Bath, Dept Chem, Bath BA2 7AY, Avon, England.
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- Katona, Gergely, 1975 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology,Univ Gothenburg, Dept Chem & Biol, S-41296 Gothenburg, Sweden.
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- Prentice, E. (författare)
- Univ Waikato, Sch Sci, Hamilton 3216, New Zealand.
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- Arcus, V. L. (författare)
- Univ Waikato, Sch Sci, Hamilton 3216, New Zealand.
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van der Kamp, M. W. (författare)
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- Pudney, C. R. (författare)
- Univ Bath, Dept Biol & Biochem, Bath BA2 7AY, Avon, England.
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Univ Bath, Dept Biol & Biochem, Bath BA2 7AY, Avon, England Univ Bath, Dept Chem, Bath BA2 7AY, Avon, England. (creator_code:org_t)
- 2021-11-29
- 2021
- Engelska.
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Ingår i: ACS Catalysis. - : American Chemical Society (ACS). - 2155-5435. ; 11:24, s. 14854-14863
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Abstract
Ämnesord
Stäng
- Uncovering the role of global protein dynamics in enzyme turnover is needed to fully understand enzyme catalysis. Recently, we have demonstrated that the heat capacity of catalysis, ΔCP‡, can reveal links between the protein free energy landscape, global protein dynamics, and enzyme turnover, suggesting that subtle changes in molecular interactions at the active site can affect long-range protein dynamics and link to enzyme temperature activity. Here, we use a model promiscuous enzyme (glucose dehydrogenase from Sulfolobus solfataricus) to chemically map how individual substrate interactions affect the temperature dependence of enzyme activity and the network of motions throughout the protein. Utilizing a combination of kinetics, red edge excitation shift (REES) spectroscopy, and computational simulation, we explore the complex relationship between enzyme–substrate interactions and the global dynamics of the protein. We find that changes in ΔCP‡ and protein dynamics can be mapped to specific substrate–enzyme interactions. Our study reveals how subtle changes in substrate binding affect global changes in motion and flexibility extending throughout the protein. © 2021 The Authors. Published by American Chemical Society
Ämnesord
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
- TEKNIK OCH TEKNOLOGIER -- Industriell bioteknik -- Biokatalys och enzymteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Industrial Biotechnology -- Biocatalysis and Enzyme Technology (hsv//eng)
Nyckelord
- catalysis
- enzyme
- MMRT
- molecular dynamics
- protein dynamics
- temperature dependence
- Enzyme activity
- Free energy
- Red Shift
- Specific heat
- Temperature distribution
- Active site
- Chemical mapping
- Enzyme catalysis
- Enzyme temperature
- Free energy landscape
- Protein-free
- Site interaction
- enzyme
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas
- Av författaren/redakt...
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Winter, S. D.
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Jones, H. B. L.
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Răsădean, D. M.
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Crean, Rory M.
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Danson, M. J.
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Pantoş, G. D.
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visa fler...
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Katona, Gergely, ...
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Prentice, E.
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Arcus, V. L.
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van der Kamp, M. ...
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Pudney, C. R.
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visa färre...
- Om ämnet
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- NATURVETENSKAP
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NATURVETENSKAP
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och Kemi
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- NATURVETENSKAP
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NATURVETENSKAP
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och Biologi
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och Biokemi och mole ...
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- TEKNIK OCH TEKNOLOGIER
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TEKNIK OCH TEKNO ...
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och Industriell biot ...
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och Biokatalys och e ...
- Artiklar i publikationen
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ACS Catalysis
- Av lärosätet
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Göteborgs universitet
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Uppsala universitet