Esterase LpEst1 from Lactobacillus plantarum: a novel and atypical member of the αβ hydrolase superfamily of enzymes.

The genome of the lactic acid bacterium Lactobacillus plantarum WCFS1 reveals the presence of a rich repertoire of esterases and lipases highlighting their important role in cellular metabolism. Among them is the carboxylesterase LpEst1 a bacterial enzyme related to the mammalian hormone-sensitive l...

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Autores principales:	Yanaisis Alvarez, María Esteban-Torres, Alvaro Cortés-Cabrera, Federico Gago, Iván Acebrón, Rocío Benavente, Karin Mardo, Blanca de Las Rivas, Rosario Muñoz, José M Mancheño
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/dc5b6ddaa163440da1caddd2d10b7909
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spelling	oai:doaj.org-article:dc5b6ddaa163440da1caddd2d10b79092021-11-18T08:26:34ZEsterase LpEst1 from Lactobacillus plantarum: a novel and atypical member of the αβ hydrolase superfamily of enzymes.1932-620310.1371/journal.pone.0092257https://doaj.org/article/dc5b6ddaa163440da1caddd2d10b79092014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24663330/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The genome of the lactic acid bacterium Lactobacillus plantarum WCFS1 reveals the presence of a rich repertoire of esterases and lipases highlighting their important role in cellular metabolism. Among them is the carboxylesterase LpEst1 a bacterial enzyme related to the mammalian hormone-sensitive lipase, which is known to play a central role in energy homeostasis. In this study, the crystal structure of LpEst1 has been determined at 2.05 Å resolution; it exhibits an αβ-hydrolase fold, consisting of a central β-sheet surrounded by α-helices, endowed with novel topological features. The structure reveals a dimeric assembly not comparable with any other enzyme from the bacterial hormone-sensitive lipase family, probably echoing the specific structural features of the participating subunits. Biophysical studies including analytical gel filtration and ultracentrifugation support the dimeric nature of LpEst1. Structural and mutational analyses of the substrate-binding pocket and active site together with biochemical studies provided insights for understanding the substrate profile of LpEst1 and suggested for the first time the conserved Asp173, which is adjacent to the nucleophile, as a key element in the stabilization of the loop where the oxyanion hole resides.Yanaisis AlvarezMaría Esteban-TorresAlvaro Cortés-CabreraFederico GagoIván AcebrónRocío BenaventeKarin MardoBlanca de Las RivasRosario MuñozJosé M MancheñoPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 3, p e92257 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Yanaisis Alvarez María Esteban-Torres Alvaro Cortés-Cabrera Federico Gago Iván Acebrón Rocío Benavente Karin Mardo Blanca de Las Rivas Rosario Muñoz José M Mancheño Esterase LpEst1 from Lactobacillus plantarum: a novel and atypical member of the αβ hydrolase superfamily of enzymes.
description	The genome of the lactic acid bacterium Lactobacillus plantarum WCFS1 reveals the presence of a rich repertoire of esterases and lipases highlighting their important role in cellular metabolism. Among them is the carboxylesterase LpEst1 a bacterial enzyme related to the mammalian hormone-sensitive lipase, which is known to play a central role in energy homeostasis. In this study, the crystal structure of LpEst1 has been determined at 2.05 Å resolution; it exhibits an αβ-hydrolase fold, consisting of a central β-sheet surrounded by α-helices, endowed with novel topological features. The structure reveals a dimeric assembly not comparable with any other enzyme from the bacterial hormone-sensitive lipase family, probably echoing the specific structural features of the participating subunits. Biophysical studies including analytical gel filtration and ultracentrifugation support the dimeric nature of LpEst1. Structural and mutational analyses of the substrate-binding pocket and active site together with biochemical studies provided insights for understanding the substrate profile of LpEst1 and suggested for the first time the conserved Asp173, which is adjacent to the nucleophile, as a key element in the stabilization of the loop where the oxyanion hole resides.
format	article
author	Yanaisis Alvarez María Esteban-Torres Alvaro Cortés-Cabrera Federico Gago Iván Acebrón Rocío Benavente Karin Mardo Blanca de Las Rivas Rosario Muñoz José M Mancheño
author_facet	Yanaisis Alvarez María Esteban-Torres Alvaro Cortés-Cabrera Federico Gago Iván Acebrón Rocío Benavente Karin Mardo Blanca de Las Rivas Rosario Muñoz José M Mancheño
author_sort	Yanaisis Alvarez
title	Esterase LpEst1 from Lactobacillus plantarum: a novel and atypical member of the αβ hydrolase superfamily of enzymes.
title_short	Esterase LpEst1 from Lactobacillus plantarum: a novel and atypical member of the αβ hydrolase superfamily of enzymes.
title_full	Esterase LpEst1 from Lactobacillus plantarum: a novel and atypical member of the αβ hydrolase superfamily of enzymes.
title_fullStr	Esterase LpEst1 from Lactobacillus plantarum: a novel and atypical member of the αβ hydrolase superfamily of enzymes.
title_full_unstemmed	Esterase LpEst1 from Lactobacillus plantarum: a novel and atypical member of the αβ hydrolase superfamily of enzymes.
title_sort	esterase lpest1 from lactobacillus plantarum: a novel and atypical member of the αβ hydrolase superfamily of enzymes.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/dc5b6ddaa163440da1caddd2d10b7909
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Esterase LpEst1 from Lactobacillus plantarum: a novel and atypical member of the αβ hydrolase superfamily of enzymes.

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