Structural and enzymatic characterization of the phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenes.

<h4>Background</h4>Organophosphates (OPs) are neurotoxic compounds for which current methods of elimination are unsatisfactory; thus bio-remediation is considered as a promising alternative. Here we provide the structural and enzymatic characterization of the recently identified enzyme i...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Guillaume Gotthard, Julien Hiblot, Daniel Gonzalez, Mikael Elias, Eric Chabriere
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/28be4c9b6b1940c59a26a9aec7e9766f
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:28be4c9b6b1940c59a26a9aec7e9766f
record_format	dspace
spelling	oai:doaj.org-article:28be4c9b6b1940c59a26a9aec7e9766f2021-11-18T08:48:36ZStructural and enzymatic characterization of the phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenes.1932-620310.1371/journal.pone.0077995https://doaj.org/article/28be4c9b6b1940c59a26a9aec7e9766f2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24223749/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>Organophosphates (OPs) are neurotoxic compounds for which current methods of elimination are unsatisfactory; thus bio-remediation is considered as a promising alternative. Here we provide the structural and enzymatic characterization of the recently identified enzyme isolated from Pseudomonas pseudoalcaligenes dubbed OPHC2. OPHC2 belongs to the metallo-β-lactamase superfamily and exhibits an unusual thermal resistance and some OP degrading abilities.<h4>Principal findings</h4>The X-ray structure of OPHC2 has been solved at 2.1 Å resolution. The enzyme is roughly globular exhibiting a αβ/βα topology typical of the metallo-β-lactamase superfamily. Several structural determinants, such as an extended dimerization surface and an intramolecular disulfide bridge, common features in thermostable enzymes, are consistent with its high Tm (97.8°C). Additionally, we provide the enzymatic characterization of OPHC2 against a wide range of OPs, esters and lactones.<h4>Significance</h4>OPHC2 possesses a broad substrate activity spectrum, since it hydrolyzes various phosphotriesters, esters, and a lactone. Because of its organophosphorus hydrolase activity, and given its intrinsic thermostability, OPHC2 is an interesting candidate for the development of an OPs bio-decontaminant. Its X-ray structure shed light on its active site, and provides key information for the understanding of the substrate binding mode and catalysis.Guillaume GotthardJulien HiblotDaniel GonzalezMikael EliasEric ChabrierePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 11, p e77995 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Guillaume Gotthard Julien Hiblot Daniel Gonzalez Mikael Elias Eric Chabriere Structural and enzymatic characterization of the phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenes.
description	<h4>Background</h4>Organophosphates (OPs) are neurotoxic compounds for which current methods of elimination are unsatisfactory; thus bio-remediation is considered as a promising alternative. Here we provide the structural and enzymatic characterization of the recently identified enzyme isolated from Pseudomonas pseudoalcaligenes dubbed OPHC2. OPHC2 belongs to the metallo-β-lactamase superfamily and exhibits an unusual thermal resistance and some OP degrading abilities.<h4>Principal findings</h4>The X-ray structure of OPHC2 has been solved at 2.1 Å resolution. The enzyme is roughly globular exhibiting a αβ/βα topology typical of the metallo-β-lactamase superfamily. Several structural determinants, such as an extended dimerization surface and an intramolecular disulfide bridge, common features in thermostable enzymes, are consistent with its high Tm (97.8°C). Additionally, we provide the enzymatic characterization of OPHC2 against a wide range of OPs, esters and lactones.<h4>Significance</h4>OPHC2 possesses a broad substrate activity spectrum, since it hydrolyzes various phosphotriesters, esters, and a lactone. Because of its organophosphorus hydrolase activity, and given its intrinsic thermostability, OPHC2 is an interesting candidate for the development of an OPs bio-decontaminant. Its X-ray structure shed light on its active site, and provides key information for the understanding of the substrate binding mode and catalysis.
format	article
author	Guillaume Gotthard Julien Hiblot Daniel Gonzalez Mikael Elias Eric Chabriere
author_facet	Guillaume Gotthard Julien Hiblot Daniel Gonzalez Mikael Elias Eric Chabriere
author_sort	Guillaume Gotthard
title	Structural and enzymatic characterization of the phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenes.
title_short	Structural and enzymatic characterization of the phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenes.
title_full	Structural and enzymatic characterization of the phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenes.
title_fullStr	Structural and enzymatic characterization of the phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenes.
title_full_unstemmed	Structural and enzymatic characterization of the phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenes.
title_sort	structural and enzymatic characterization of the phosphotriesterase ophc2 from pseudomonas pseudoalcaligenes.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/28be4c9b6b1940c59a26a9aec7e9766f
work_keys_str_mv	AT guillaumegotthard structuralandenzymaticcharacterizationofthephosphotriesteraseophc2frompseudomonaspseudoalcaligenes AT julienhiblot structuralandenzymaticcharacterizationofthephosphotriesteraseophc2frompseudomonaspseudoalcaligenes AT danielgonzalez structuralandenzymaticcharacterizationofthephosphotriesteraseophc2frompseudomonaspseudoalcaligenes AT mikaelelias structuralandenzymaticcharacterizationofthephosphotriesteraseophc2frompseudomonaspseudoalcaligenes AT ericchabriere structuralandenzymaticcharacterizationofthephosphotriesteraseophc2frompseudomonaspseudoalcaligenes
_version_	1718421251199860736

Structural and enzymatic characterization of the phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenes.

Ejemplares similares