Metagenomic mining for thermostable esterolytic enzymes uncovers a new family of bacterial esterases
Biocatalysts exerting activity against ester bonds have a broad range of applications in modern biotechnology. Here, we have identified a new esterolytic enzyme by screening a metagenomic sample collected from a hot spring in Kamchatka, Russia. Biochemical characterization of the new esterase, terme...
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ftpubmed:oai:pubmedcentral.nih.gov:5171882 2023-05-15T16:59:16+02:00 Metagenomic mining for thermostable esterolytic enzymes uncovers a new family of bacterial esterases Zarafeta, Dimitra Moschidi, Danai Ladoukakis, Efthymios Gavrilov, Sergey Chrysina, Evangelia D. Chatziioannou, Aristotelis Kublanov, Ilya Skretas, Georgios Kolisis, Fragiskos N. 2016-12-19 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5171882/ http://www.ncbi.nlm.nih.gov/pubmed/27991516 https://doi.org/10.1038/srep38886 en eng Nature Publishing Group http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5171882/ http://www.ncbi.nlm.nih.gov/pubmed/27991516 http://dx.doi.org/10.1038/srep38886 Copyright © 2016, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ CC-BY Article Text 2016 ftpubmed https://doi.org/10.1038/srep38886 2017-01-01T01:04:45Z Biocatalysts exerting activity against ester bonds have a broad range of applications in modern biotechnology. Here, we have identified a new esterolytic enzyme by screening a metagenomic sample collected from a hot spring in Kamchatka, Russia. Biochemical characterization of the new esterase, termed EstDZ2, revealed that it is highly active against medium chain fatty acid esters at temperatures between 25 and 60 °C and at pH values 7–8. The new enzyme is moderately thermostable with a half-life of more than six hours at 60 °C, but exhibits exquisite stability against high concentrations of organic solvents. Phylogenetic analysis indicated that EstDZ2 is likely an Acetothermia enzyme that belongs to a new family of bacterial esterases, for which we propose the index XV. One distinctive feature of this new family, is the presence of a conserved GHSAG catalytic motif. Multiple sequence alignment, coupled with computational modelling of the three-dimensional structure of EstDZ2, revealed that the enzyme lacks the largest part of the “cap” domain, whose extended structure is characteristic for the closely related Family IV esterases. Thus, EstDZ2 appears to be distinct from known related esterolytic enzymes, both in terms of sequence characteristics, as well as in terms of three-dimensional structure. Text Kamchatka PubMed Central (PMC) Scientific Reports 6 1 |
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Article Zarafeta, Dimitra Moschidi, Danai Ladoukakis, Efthymios Gavrilov, Sergey Chrysina, Evangelia D. Chatziioannou, Aristotelis Kublanov, Ilya Skretas, Georgios Kolisis, Fragiskos N. Metagenomic mining for thermostable esterolytic enzymes uncovers a new family of bacterial esterases |
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Biocatalysts exerting activity against ester bonds have a broad range of applications in modern biotechnology. Here, we have identified a new esterolytic enzyme by screening a metagenomic sample collected from a hot spring in Kamchatka, Russia. Biochemical characterization of the new esterase, termed EstDZ2, revealed that it is highly active against medium chain fatty acid esters at temperatures between 25 and 60 °C and at pH values 7–8. The new enzyme is moderately thermostable with a half-life of more than six hours at 60 °C, but exhibits exquisite stability against high concentrations of organic solvents. Phylogenetic analysis indicated that EstDZ2 is likely an Acetothermia enzyme that belongs to a new family of bacterial esterases, for which we propose the index XV. One distinctive feature of this new family, is the presence of a conserved GHSAG catalytic motif. Multiple sequence alignment, coupled with computational modelling of the three-dimensional structure of EstDZ2, revealed that the enzyme lacks the largest part of the “cap” domain, whose extended structure is characteristic for the closely related Family IV esterases. Thus, EstDZ2 appears to be distinct from known related esterolytic enzymes, both in terms of sequence characteristics, as well as in terms of three-dimensional structure. |
format |
Text |
author |
Zarafeta, Dimitra Moschidi, Danai Ladoukakis, Efthymios Gavrilov, Sergey Chrysina, Evangelia D. Chatziioannou, Aristotelis Kublanov, Ilya Skretas, Georgios Kolisis, Fragiskos N. |
author_facet |
Zarafeta, Dimitra Moschidi, Danai Ladoukakis, Efthymios Gavrilov, Sergey Chrysina, Evangelia D. Chatziioannou, Aristotelis Kublanov, Ilya Skretas, Georgios Kolisis, Fragiskos N. |
author_sort |
Zarafeta, Dimitra |
title |
Metagenomic mining for thermostable esterolytic enzymes uncovers a new family of bacterial esterases |
title_short |
Metagenomic mining for thermostable esterolytic enzymes uncovers a new family of bacterial esterases |
title_full |
Metagenomic mining for thermostable esterolytic enzymes uncovers a new family of bacterial esterases |
title_fullStr |
Metagenomic mining for thermostable esterolytic enzymes uncovers a new family of bacterial esterases |
title_full_unstemmed |
Metagenomic mining for thermostable esterolytic enzymes uncovers a new family of bacterial esterases |
title_sort |
metagenomic mining for thermostable esterolytic enzymes uncovers a new family of bacterial esterases |
publisher |
Nature Publishing Group |
publishDate |
2016 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5171882/ http://www.ncbi.nlm.nih.gov/pubmed/27991516 https://doi.org/10.1038/srep38886 |
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Kamchatka |
genre_facet |
Kamchatka |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5171882/ http://www.ncbi.nlm.nih.gov/pubmed/27991516 http://dx.doi.org/10.1038/srep38886 |
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Copyright © 2016, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
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CC-BY |
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https://doi.org/10.1038/srep38886 |
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