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The role of ligand-gated conformational changes in enzyme catalysis
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Biochemistry.ORCID iD: 0000-0002-6904-2511
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Biochemistry.ORCID iD: 0000-0002-1123-0413
Department of Chemistry, University at Buffalo, SUNY, Buffalo, New York 14260-3000, U.S.A.
Uppsala University, Science for Life Laboratory, SciLifeLab. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Biochemistry.ORCID iD: 0000-0002-3190-1173
2019 (English)In: Biochemical Society Transactions, ISSN 0300-5127, E-ISSN 1470-8752, Vol. 47, no 5, p. 1449-1460Article in journal (Refereed) Published
Abstract [en]

Structural and biochemical studies on diverse enzymes have highlighted the importance of ligand-gated conformational changes in enzyme catalysis, where the intrinsic binding energy of the common phosphoryl group of their substrates is used to drive energetically unfavorable conformational changes in catalytic loops, from inactive open to catalytically competent closed conformations. However, computational studies have historically been unable to capture the activating role of these conformational changes. Here, we discuss recent experimental and computational studies, which can remarkably pinpoint the role of ligand-gated conformational changes in enzyme catalysis, even when not modeling the loop dynamics explicitly. Finally, through our joint analyses of these data, we demonstrate how the synergy between theory and experiment is crucial for furthering our understanding of enzyme catalysis

Place, publisher, year, edition, pages
Portland Press, 2019. Vol. 47, no 5, p. 1449-1460
Keywords [en]
computational modeling, dianion activation, enzyme catalysis, loop dynamics, triosephosphate isomerase
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-397178DOI: 10.1042/BST20190298ISI: 000493899200020PubMedID: 31657438OAI: oai:DiVA.org:uu-397178DiVA, id: diva2:1370700
Funder
Stiftelsen Olle Engkvist Byggmästare, 190-0355Knut and Alice Wallenberg Foundation, 2018.0140Swedish Research Council, 2015-04298NIH (National Institute of Health), GM116921Available from: 2019-11-16 Created: 2019-11-16 Last updated: 2019-12-06Bibliographically approved

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