An enzyme with high catalytic proficiency utilizes distal site substrate binding energy to stabilize the closed state but at the expense of substrate inhibition

Robertson, A., Cruz-Navarrete, F.A., Wood, H. et al. (6 more authors) (2022) An enzyme with high catalytic proficiency utilizes distal site substrate binding energy to stabilize the closed state but at the expense of substrate inhibition. ACS Catalysis, 12 (5). pp. 3149-3164. ISSN 2155-5435

Abstract

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Authors/Creators:
Copyright, Publisher and Additional Information: © 2022 American Chemical Society. This is an Open Access article distributed under the terms of the Creative Commons Attribution Licence (http://creativecommons.org/licenses/by/4.0)
Keywords: Enzyme catalytic proficiency; Phosphoryl transfer mechanism; Transition state analogue; X-ray crystallography; NMR spectroscopy
Dates:
  • Accepted: 14 February 2022
  • Published (online): 22 February 2022
  • Published: 4 March 2022
Institution: The University of Sheffield
Academic Units: The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield)
Funding Information:
FunderGrant number
HIGHER EDUCATION FUNDING COUNCIL FOR ENGLANDUNSPECIFIED
WELLCOME TRUST (THE)087850/Z/08/Z
BIOTECHNOLOGY AND BIOLOGICAL SCIENCES RESEARCH COUNCILBB/E017541/1
BIOTECHNOLOGY AND BIOLOGICAL SCIENCES RESEARCH COUNCILBB/I002146/1
ENGINEERING AND PHYSICAL SCIENCE RESEARCH COUNCILEP/S01358X/1
BIOTECHNOLOGY AND BIOLOGICAL SCIENCES RESEARCH COUNCILBB/R000727/1
Depositing User: Symplectic Sheffield
Date Deposited: 23 Feb 2022 12:49
Last Modified: 10 Feb 2023 14:12
Status: Published
Publisher: American Chemical Society
Refereed: Yes
Identification Number: https://doi.org/10.1021/acscatal.1c05524

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