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

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Item Type: Article
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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:
  • Published: 4 March 2022
  • Published (online): 22 February 2022
  • Accepted: 14 February 2022
Institution: The University of Sheffield
Academic Units: The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield)
Funding Information:
Funder
Grant number
HIGHER EDUCATION FUNDING COUNCIL FOR ENGLAND
UNSPECIFIED
WELLCOME TRUST (THE)
087850/Z/08/Z
BIOTECHNOLOGY AND BIOLOGICAL SCIENCES RESEARCH COUNCIL
BB/E017541/1
BIOTECHNOLOGY AND BIOLOGICAL SCIENCES RESEARCH COUNCIL
BB/I002146/1
ENGINEERING AND PHYSICAL SCIENCE RESEARCH COUNCIL
EP/S01358X/1
BIOTECHNOLOGY AND BIOLOGICAL SCIENCES RESEARCH COUNCIL
BB/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: 10.1021/acscatal.1c05524
Open Archives Initiative ID (OAI ID):

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