Chemical Mapping Exposes the Importance of Active Site Interactions in Governing the Temperature Dependence of Enzyme Turnover-Reference-Cited by-同舟云学术

Chemical Mapping Exposes the Importance of Active Site Interactions in Governing the Temperature Dependence of Enzyme Turnover

Published:2021-11-29 Issue:24 Volume:11 Page:14854-14863
ISSN:2155-5435
Container-title:ACS Catalysis
language:en
Short-container-title:ACS Catal.

Author:

Winter Samuel D.¹,Jones Hannah B. L.¹,Răsădean Dora M.²,Crean Rory M.³,Danson Michael J.¹,Pantoş G. Dan²,Katona Gergely⁴,Prentice Erica⁵^ORCID,Arcus Vickery L.⁵,van der Kamp Marc W.⁶^ORCID,Pudney Christopher R.¹^ORCID

Affiliation:

1. Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, U.K.

2. Department of Chemistry, University of Bath, Bath BA2 7AY, U.K.

3. Science for Life Laboratory, Department of Chemistry − BMC, Uppsala University, Uppsala 752 37, Sweden

4. Department of Chemistry and Biology, University of Gothenburg, Göteborg 412 96, Sweden

5. School of Science, University of Waikato, Hamilton 3216, New Zealand

6. Department of Biochemistry, University of Bristol, Bristol BS8 1TD, U.K.

Funder

Engineering and Physical Sciences Research Council

Biotechnology and Biological Sciences Research Council

Publisher

American Chemical Society (ACS)

Subject

Catalysis,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acscatal.1c04679

Reference40 articles.

1. Uncovering the Relationship between the Change in Heat Capacity for Enzyme Catalysis and Vibrational Frequency through Isotope Effect Studies

2. Cooperativity and flexibility in enzyme evolution

3. Unraveling the role of protein dynamics in dihydrofolate reductase catalysis

4. Good vibrations in enzyme-catalysed reactions

5. Establishment of mesophilic-like catalytic properties in a thermophilic enzyme without affecting its thermal stability

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