Secretory Phospholipases A(2) in Plants

Secreted phospholipases (sPLA(2)s) in plants are a growing group of enzymes that catalyze the hydrolysis of sn-2 glycerophospholipids to lysophospholipids and free fatty acids. Until today, around only 20 sPLA(2)s were reported from plants. This review discusses the newly acquired information on pla...

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Detalles Bibliográficos
Autores principales: Mariani, María Elisa, Fidelio, Gerardo Daniel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2019
Materias:
Plant Science
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6635587/
https://www.ncbi.nlm.nih.gov/pubmed/31354755
http://dx.doi.org/10.3389/fpls.2019.00861
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author Mariani, María Elisa
Fidelio, Gerardo Daniel
author_facet Mariani, María Elisa
Fidelio, Gerardo Daniel
author_sort Mariani, María Elisa
collection PubMed
description Secreted phospholipases (sPLA(2)s) in plants are a growing group of enzymes that catalyze the hydrolysis of sn-2 glycerophospholipids to lysophospholipids and free fatty acids. Until today, around only 20 sPLA(2)s were reported from plants. This review discusses the newly acquired information on plant sPLA(2)s including molecular, biochemical, catalytic, and functional aspects. The comparative analysis also includes phylogenetic, evolutionary, and tridimensional structure. The observations with emphasis in Glycine max sPLA(2) are compared with the available data reported for all plants sPLA(2)s and with those described for animals (mainly from pancreatic juice and venoms sources).
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spelling pubmed-66355872019-07-26 Secretory Phospholipases A(2) in Plants Mariani, María Elisa Fidelio, Gerardo Daniel Front Plant Sci Plant Science Secreted phospholipases (sPLA(2)s) in plants are a growing group of enzymes that catalyze the hydrolysis of sn-2 glycerophospholipids to lysophospholipids and free fatty acids. Until today, around only 20 sPLA(2)s were reported from plants. This review discusses the newly acquired information on plant sPLA(2)s including molecular, biochemical, catalytic, and functional aspects. The comparative analysis also includes phylogenetic, evolutionary, and tridimensional structure. The observations with emphasis in Glycine max sPLA(2) are compared with the available data reported for all plants sPLA(2)s and with those described for animals (mainly from pancreatic juice and venoms sources). Frontiers Media S.A. 2019-07-10 /pmc/articles/PMC6635587/ /pubmed/31354755 http://dx.doi.org/10.3389/fpls.2019.00861 Text en Copyright © 2019 Mariani and Fidelio. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Mariani, María Elisa
Fidelio, Gerardo Daniel
Secretory Phospholipases A(2) in Plants
title Secretory Phospholipases A(2) in Plants
title_full Secretory Phospholipases A(2) in Plants
title_fullStr Secretory Phospholipases A(2) in Plants
title_full_unstemmed Secretory Phospholipases A(2) in Plants
title_short Secretory Phospholipases A(2) in Plants
title_sort secretory phospholipases a(2) in plants
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6635587/
https://www.ncbi.nlm.nih.gov/pubmed/31354755
http://dx.doi.org/10.3389/fpls.2019.00861
work_keys_str_mv AT marianimariaelisa secretoryphospholipasesa2inplants
AT fideliogerardodaniel secretoryphospholipasesa2inplants

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