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Linking Protein Motion to Enzyme Catalysis
Enzyme motions on a broad range of time scales can play an important role in various intra- and intermolecular events, including substrate binding, catalysis of the chemical conversion, and product release. The relationship between protein motions and catalytic activity is of contemporary interest i...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4341894/ https://www.ncbi.nlm.nih.gov/pubmed/25591120 http://dx.doi.org/10.3390/molecules20011192 |
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author | Singh, Priyanka Abeysinghe, Thelma Kohen, Amnon |
author_facet | Singh, Priyanka Abeysinghe, Thelma Kohen, Amnon |
author_sort | Singh, Priyanka |
collection | PubMed |
description | Enzyme motions on a broad range of time scales can play an important role in various intra- and intermolecular events, including substrate binding, catalysis of the chemical conversion, and product release. The relationship between protein motions and catalytic activity is of contemporary interest in enzymology. To understand the factors influencing the rates of enzyme-catalyzed reactions, the dynamics of the protein-solvent-ligand complex must be considered. The current review presents two case studies of enzymes—dihydrofolate reductase (DHFR) and thymidylate synthase (TSase)—and discusses the role of protein motions in their catalyzed reactions. Specifically, we will discuss the utility of kinetic isotope effects (KIEs) and their temperature dependence as tools in probing such phenomena. |
format | Online Article Text |
id | pubmed-4341894 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-43418942016-01-13 Linking Protein Motion to Enzyme Catalysis Singh, Priyanka Abeysinghe, Thelma Kohen, Amnon Molecules Review Enzyme motions on a broad range of time scales can play an important role in various intra- and intermolecular events, including substrate binding, catalysis of the chemical conversion, and product release. The relationship between protein motions and catalytic activity is of contemporary interest in enzymology. To understand the factors influencing the rates of enzyme-catalyzed reactions, the dynamics of the protein-solvent-ligand complex must be considered. The current review presents two case studies of enzymes—dihydrofolate reductase (DHFR) and thymidylate synthase (TSase)—and discusses the role of protein motions in their catalyzed reactions. Specifically, we will discuss the utility of kinetic isotope effects (KIEs) and their temperature dependence as tools in probing such phenomena. MDPI 2015-01-13 /pmc/articles/PMC4341894/ /pubmed/25591120 http://dx.doi.org/10.3390/molecules20011192 Text en © 2015 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Singh, Priyanka Abeysinghe, Thelma Kohen, Amnon Linking Protein Motion to Enzyme Catalysis |
title | Linking Protein Motion to Enzyme Catalysis |
title_full | Linking Protein Motion to Enzyme Catalysis |
title_fullStr | Linking Protein Motion to Enzyme Catalysis |
title_full_unstemmed | Linking Protein Motion to Enzyme Catalysis |
title_short | Linking Protein Motion to Enzyme Catalysis |
title_sort | linking protein motion to enzyme catalysis |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4341894/ https://www.ncbi.nlm.nih.gov/pubmed/25591120 http://dx.doi.org/10.3390/molecules20011192 |
work_keys_str_mv | AT singhpriyanka linkingproteinmotiontoenzymecatalysis AT abeysinghethelma linkingproteinmotiontoenzymecatalysis AT kohenamnon linkingproteinmotiontoenzymecatalysis |