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Updating Phospholipase A(2) Biology

The phospholipase A(2) (PLA(2)) superfamily contains more than 50 enzymes in mammals that are subdivided into several distinct families on a structural and biochemical basis. In principle, PLA(2) has the capacity to hydrolyze the sn-2 position of glycerophospholipids to release fatty acids and lysop...

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Detalles Bibliográficos
Autores principales: Murakami, Makoto, Sato, Hiroyasu, Taketomi, Yoshitaka
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7603386/
https://www.ncbi.nlm.nih.gov/pubmed/33086624
http://dx.doi.org/10.3390/biom10101457
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author Murakami, Makoto
Sato, Hiroyasu
Taketomi, Yoshitaka
author_facet Murakami, Makoto
Sato, Hiroyasu
Taketomi, Yoshitaka
author_sort Murakami, Makoto
collection PubMed
description The phospholipase A(2) (PLA(2)) superfamily contains more than 50 enzymes in mammals that are subdivided into several distinct families on a structural and biochemical basis. In principle, PLA(2) has the capacity to hydrolyze the sn-2 position of glycerophospholipids to release fatty acids and lysophospholipids, yet several enzymes in this superfamily catalyze other reactions rather than or in addition to the PLA(2) reaction. PLA(2) enzymes play crucial roles in not only the production of lipid mediators, but also membrane remodeling, bioenergetics, and body surface barrier, thereby participating in a number of biological events. Accordingly, disturbance of PLA(2)-regulated lipid metabolism is often associated with various diseases. This review updates the current state of understanding of the classification, enzymatic properties, and biological functions of various enzymes belonging to the PLA(2) superfamily, focusing particularly on the novel roles of PLA(2)s in vivo.
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spelling pubmed-76033862020-11-01 Updating Phospholipase A(2) Biology Murakami, Makoto Sato, Hiroyasu Taketomi, Yoshitaka Biomolecules Review The phospholipase A(2) (PLA(2)) superfamily contains more than 50 enzymes in mammals that are subdivided into several distinct families on a structural and biochemical basis. In principle, PLA(2) has the capacity to hydrolyze the sn-2 position of glycerophospholipids to release fatty acids and lysophospholipids, yet several enzymes in this superfamily catalyze other reactions rather than or in addition to the PLA(2) reaction. PLA(2) enzymes play crucial roles in not only the production of lipid mediators, but also membrane remodeling, bioenergetics, and body surface barrier, thereby participating in a number of biological events. Accordingly, disturbance of PLA(2)-regulated lipid metabolism is often associated with various diseases. This review updates the current state of understanding of the classification, enzymatic properties, and biological functions of various enzymes belonging to the PLA(2) superfamily, focusing particularly on the novel roles of PLA(2)s in vivo. MDPI 2020-10-19 /pmc/articles/PMC7603386/ /pubmed/33086624 http://dx.doi.org/10.3390/biom10101457 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
Murakami, Makoto
Sato, Hiroyasu
Taketomi, Yoshitaka
Updating Phospholipase A(2) Biology
title Updating Phospholipase A(2) Biology
title_full Updating Phospholipase A(2) Biology
title_fullStr Updating Phospholipase A(2) Biology
title_full_unstemmed Updating Phospholipase A(2) Biology
title_short Updating Phospholipase A(2) Biology
title_sort updating phospholipase a(2) biology
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7603386/
https://www.ncbi.nlm.nih.gov/pubmed/33086624
http://dx.doi.org/10.3390/biom10101457
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