The role of ligand-gated conformational changes in enzyme catalysis
| Autor: | John P. Richard, Ana R. Calixto, Cátia Moreira, Shina Caroline Lynn Kamerlin |
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| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
computational modeling
Protein Conformation Biophysics 010402 general chemistry loop dynamics Ligands 01 natural sciences Biochemistry enzyme catalysis Catalysis Enzyme catalysis Triosephosphate isomerase 03 medical and health sciences Structural Biology Chemical Biology Computer Simulation Review Articles chemistry.chemical_classification 0303 health sciences Chemistry dianion activation 030302 biochemistry & molecular biology Biochemistry and Molecular Biology Computational Biology 0104 chemical sciences Enzymes triosephosphate isomerase Enzyme Enzymology Ligand-gated ion channel sense organs Ion Channel Gating Biokemi och molekylärbiologi |
| Zdroj: | Biochemical Society Transactions |
| ISSN: | 1470-8752 0300-5127 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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