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Characterisation of a New Family of Carboxyl Esterases with an OsmC Domain
Proteins in the serine esterase family are widely distributed in bacterial phyla and display activity against a range of biologically produced and chemically synthesized esters. A serine esterase from the psychrophilic bacterium Pseudoalteromonas arctica with a C-terminal OsmC-like domain was recent...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5113044/ https://www.ncbi.nlm.nih.gov/pubmed/27851780 http://dx.doi.org/10.1371/journal.pone.0166128 |
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author | Jensen, Mai-Britt V. Horsfall, Louise E. Wardrope, Caroline Togneri, Peter D. Marles-Wright, Jon Rosser, Susan J. |
author_facet | Jensen, Mai-Britt V. Horsfall, Louise E. Wardrope, Caroline Togneri, Peter D. Marles-Wright, Jon Rosser, Susan J. |
author_sort | Jensen, Mai-Britt V. |
collection | PubMed |
description | Proteins in the serine esterase family are widely distributed in bacterial phyla and display activity against a range of biologically produced and chemically synthesized esters. A serine esterase from the psychrophilic bacterium Pseudoalteromonas arctica with a C-terminal OsmC-like domain was recently characterized; here we report on the identification and characterization of further putative esterases with OsmC-like domains constituting a new esterase family that is found in a variety of bacterial species from different environmental niches. All of these proteins contained the Ser-Asp-His motif common to serine esterases and a highly conserved pentapeptide nucleophilic elbow motif. We produced these proteins heterologously in Escherichia coli and demonstrated their activity against a range of esterase substrates. Two of the esterases characterized have activity of over two orders of magnitude higher than other members of the family, and are active over a wide temperature range. We determined the crystal structure of the esterase domain of the protein from Rhodothermus marinus and show that it conforms to the classical α/β hydrolase fold with an extended ‘lid’ region, which occludes the active site of the protein in the crystal. The expansion of characterized members of the esterase family and demonstration of activity over a wide-range of temperatures could be of use in biotechnological applications such as the pharmaceutical, detergent, bioremediation and dairy industries. |
format | Online Article Text |
id | pubmed-5113044 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-51130442016-12-08 Characterisation of a New Family of Carboxyl Esterases with an OsmC Domain Jensen, Mai-Britt V. Horsfall, Louise E. Wardrope, Caroline Togneri, Peter D. Marles-Wright, Jon Rosser, Susan J. PLoS One Research Article Proteins in the serine esterase family are widely distributed in bacterial phyla and display activity against a range of biologically produced and chemically synthesized esters. A serine esterase from the psychrophilic bacterium Pseudoalteromonas arctica with a C-terminal OsmC-like domain was recently characterized; here we report on the identification and characterization of further putative esterases with OsmC-like domains constituting a new esterase family that is found in a variety of bacterial species from different environmental niches. All of these proteins contained the Ser-Asp-His motif common to serine esterases and a highly conserved pentapeptide nucleophilic elbow motif. We produced these proteins heterologously in Escherichia coli and demonstrated their activity against a range of esterase substrates. Two of the esterases characterized have activity of over two orders of magnitude higher than other members of the family, and are active over a wide temperature range. We determined the crystal structure of the esterase domain of the protein from Rhodothermus marinus and show that it conforms to the classical α/β hydrolase fold with an extended ‘lid’ region, which occludes the active site of the protein in the crystal. The expansion of characterized members of the esterase family and demonstration of activity over a wide-range of temperatures could be of use in biotechnological applications such as the pharmaceutical, detergent, bioremediation and dairy industries. Public Library of Science 2016-11-16 /pmc/articles/PMC5113044/ /pubmed/27851780 http://dx.doi.org/10.1371/journal.pone.0166128 Text en © 2016 Jensen et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Jensen, Mai-Britt V. Horsfall, Louise E. Wardrope, Caroline Togneri, Peter D. Marles-Wright, Jon Rosser, Susan J. Characterisation of a New Family of Carboxyl Esterases with an OsmC Domain |
title | Characterisation of a New Family of Carboxyl Esterases with an OsmC Domain |
title_full | Characterisation of a New Family of Carboxyl Esterases with an OsmC Domain |
title_fullStr | Characterisation of a New Family of Carboxyl Esterases with an OsmC Domain |
title_full_unstemmed | Characterisation of a New Family of Carboxyl Esterases with an OsmC Domain |
title_short | Characterisation of a New Family of Carboxyl Esterases with an OsmC Domain |
title_sort | characterisation of a new family of carboxyl esterases with an osmc domain |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5113044/ https://www.ncbi.nlm.nih.gov/pubmed/27851780 http://dx.doi.org/10.1371/journal.pone.0166128 |
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