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Fatty Acid Allosteric Regulation of C-H Activation in Plant and Animal Lipoxygenases

Lipoxygenases (LOXs) catalyze the (per) oxidation of fatty acids that serve as important mediators for cell signaling and inflammation. These reactions are initiated by a C-H activation step that is allosterically regulated in plant and animal enzymes. LOXs from higher eukaryotes are equipped with a...

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Autores principales: Offenbacher, Adam R., Holman, Theodore R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7436259/
https://www.ncbi.nlm.nih.gov/pubmed/32722330
http://dx.doi.org/10.3390/molecules25153374
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author Offenbacher, Adam R.
Holman, Theodore R.
author_facet Offenbacher, Adam R.
Holman, Theodore R.
author_sort Offenbacher, Adam R.
collection PubMed
description Lipoxygenases (LOXs) catalyze the (per) oxidation of fatty acids that serve as important mediators for cell signaling and inflammation. These reactions are initiated by a C-H activation step that is allosterically regulated in plant and animal enzymes. LOXs from higher eukaryotes are equipped with an N-terminal PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain that has been implicated to bind to small molecule allosteric effectors, which in turn modulate substrate specificity and the rate-limiting steps of catalysis. Herein, the kinetic and structural evidence that describes the allosteric regulation of plant and animal lipoxygenase chemistry by fatty acids and their derivatives are summarized.
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spelling pubmed-74362592020-08-24 Fatty Acid Allosteric Regulation of C-H Activation in Plant and Animal Lipoxygenases Offenbacher, Adam R. Holman, Theodore R. Molecules Review Lipoxygenases (LOXs) catalyze the (per) oxidation of fatty acids that serve as important mediators for cell signaling and inflammation. These reactions are initiated by a C-H activation step that is allosterically regulated in plant and animal enzymes. LOXs from higher eukaryotes are equipped with an N-terminal PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain that has been implicated to bind to small molecule allosteric effectors, which in turn modulate substrate specificity and the rate-limiting steps of catalysis. Herein, the kinetic and structural evidence that describes the allosteric regulation of plant and animal lipoxygenase chemistry by fatty acids and their derivatives are summarized. MDPI 2020-07-24 /pmc/articles/PMC7436259/ /pubmed/32722330 http://dx.doi.org/10.3390/molecules25153374 Text en © 2020 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 (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Offenbacher, Adam R.
Holman, Theodore R.
Fatty Acid Allosteric Regulation of C-H Activation in Plant and Animal Lipoxygenases
title Fatty Acid Allosteric Regulation of C-H Activation in Plant and Animal Lipoxygenases
title_full Fatty Acid Allosteric Regulation of C-H Activation in Plant and Animal Lipoxygenases
title_fullStr Fatty Acid Allosteric Regulation of C-H Activation in Plant and Animal Lipoxygenases
title_full_unstemmed Fatty Acid Allosteric Regulation of C-H Activation in Plant and Animal Lipoxygenases
title_short Fatty Acid Allosteric Regulation of C-H Activation in Plant and Animal Lipoxygenases
title_sort fatty acid allosteric regulation of c-h activation in plant and animal lipoxygenases
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7436259/
https://www.ncbi.nlm.nih.gov/pubmed/32722330
http://dx.doi.org/10.3390/molecules25153374
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