Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15
Esterases represent an important class of enzymes with a wide variety of industrial applications. A novel hormone-sensitive lipase (HSL) family esterase, Est19, from the Antarctic bacterium Pseudomonas sp. E2-15 is identified, cloned, and expressed. The enzyme possesses a GESAG motif containing an a...
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ftmdpi:oai:mdpi.com:/2218-273X/11/11/1552/ 2023-08-20T04:01:14+02:00 Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15 Xiaoyu Liu Mingyang Zhou Shu Xing Tao Wu Hailun He John Kevin Bielicki Jianbin Chen agris 2021-10-20 application/pdf https://doi.org/10.3390/biom11111552 EN eng Multidisciplinary Digital Publishing Institute Cellular Biochemistry https://dx.doi.org/10.3390/biom11111552 https://creativecommons.org/licenses/by/4.0/ Biomolecules; Volume 11; Issue 11; Pages: 1552 esterase Antarctic HSL family GESAG motif Text 2021 ftmdpi https://doi.org/10.3390/biom11111552 2023-08-01T03:00:40Z Esterases represent an important class of enzymes with a wide variety of industrial applications. A novel hormone-sensitive lipase (HSL) family esterase, Est19, from the Antarctic bacterium Pseudomonas sp. E2-15 is identified, cloned, and expressed. The enzyme possesses a GESAG motif containing an active serine (S) located within a highly conserved catalytic triad of Ser155, Asp253, and His282 residues. The catalytic efficiency (kcat/Km) of Est19 for the pNPC6 substrate is 148.68 s−1mM−1 at 40 °C. Replacing Glu154 juxtaposed to the critical catalytic serine with Asp (E154→D substitution) reduced the activity and catalytic efficiency of the enzyme two-fold, with little change in the substrate affinity. The wild-type enzyme retained near complete activity over a temperature range of 10–60 °C, while ~50% of its activity was retained at 0 °C. A phylogenetic analysis suggested that Est19 and its homologs may represent a new subfamily of HSL. The thermal stability and stereo-specificity suggest that the Est19 esterase may be useful for cold and chiral catalyses. Text Antarc* Antarctic MDPI Open Access Publishing Antarctic The Antarctic Biomolecules 11 11 1552 |
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MDPI Open Access Publishing |
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ftmdpi |
language |
English |
topic |
esterase Antarctic HSL family GESAG motif |
spellingShingle |
esterase Antarctic HSL family GESAG motif Xiaoyu Liu Mingyang Zhou Shu Xing Tao Wu Hailun He John Kevin Bielicki Jianbin Chen Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15 |
topic_facet |
esterase Antarctic HSL family GESAG motif |
description |
Esterases represent an important class of enzymes with a wide variety of industrial applications. A novel hormone-sensitive lipase (HSL) family esterase, Est19, from the Antarctic bacterium Pseudomonas sp. E2-15 is identified, cloned, and expressed. The enzyme possesses a GESAG motif containing an active serine (S) located within a highly conserved catalytic triad of Ser155, Asp253, and His282 residues. The catalytic efficiency (kcat/Km) of Est19 for the pNPC6 substrate is 148.68 s−1mM−1 at 40 °C. Replacing Glu154 juxtaposed to the critical catalytic serine with Asp (E154→D substitution) reduced the activity and catalytic efficiency of the enzyme two-fold, with little change in the substrate affinity. The wild-type enzyme retained near complete activity over a temperature range of 10–60 °C, while ~50% of its activity was retained at 0 °C. A phylogenetic analysis suggested that Est19 and its homologs may represent a new subfamily of HSL. The thermal stability and stereo-specificity suggest that the Est19 esterase may be useful for cold and chiral catalyses. |
format |
Text |
author |
Xiaoyu Liu Mingyang Zhou Shu Xing Tao Wu Hailun He John Kevin Bielicki Jianbin Chen |
author_facet |
Xiaoyu Liu Mingyang Zhou Shu Xing Tao Wu Hailun He John Kevin Bielicki Jianbin Chen |
author_sort |
Xiaoyu Liu |
title |
Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15 |
title_short |
Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15 |
title_full |
Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15 |
title_fullStr |
Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15 |
title_full_unstemmed |
Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15 |
title_sort |
identification and biochemical characterization of a novel hormone-sensitive lipase family esterase est19 from the antarctic bacterium pseudomonas sp. e2-15 |
publisher |
Multidisciplinary Digital Publishing Institute |
publishDate |
2021 |
url |
https://doi.org/10.3390/biom11111552 |
op_coverage |
agris |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Biomolecules; Volume 11; Issue 11; Pages: 1552 |
op_relation |
Cellular Biochemistry https://dx.doi.org/10.3390/biom11111552 |
op_rights |
https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.3390/biom11111552 |
container_title |
Biomolecules |
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11 |
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11 |
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1552 |
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1774723644108308480 |