Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium <i>Pseudomonas</i> 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 <i>Pseudomonas</i> sp. E2-15 is identified, cloned, and expressed. The enzyme possesses a GESAG mo...

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Autores principales:	Xiaoyu Liu, Mingyang Zhou, Shu Xing, Tao Wu, Hailun He, John Kevin Bielicki, Jianbin Chen
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	esterase Antarctic HSL family GESAG motif Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/26af0279e2d143e193f8ad781c2465ab
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spelling	oai:doaj.org-article:26af0279e2d143e193f8ad781c2465ab2021-11-25T16:51:42ZIdentification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium <i>Pseudomonas</i> sp. E2-1510.3390/biom111115522218-273Xhttps://doaj.org/article/26af0279e2d143e193f8ad781c2465ab2021-10-01T00:00:00Zhttps://www.mdpi.com/2218-273X/11/11/1552https://doaj.org/toc/2218-273XEsterases 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 <i>Pseudomonas</i> 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 Ser<sup>155</sup>, Asp<sup>253</sup>, and His<sup>282</sup> residues. The catalytic efficiency (<i>k</i><sub>cat</sub>/<i>K</i><sub>m</sub>) of Est19 for the <i>p</i>NPC6 substrate is 148.68 s<sup>−1</sup>mM<sup>−1</sup> at 40 °C. Replacing Glu<sup>154</sup> 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.Xiaoyu LiuMingyang ZhouShu XingTao WuHailun HeJohn Kevin BielickiJianbin ChenMDPI AGarticleesteraseAntarcticHSL familyGESAG motifMicrobiologyQR1-502ENBiomolecules, Vol 11, Iss 1552, p 1552 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	esterase Antarctic HSL family GESAG motif Microbiology QR1-502
spellingShingle	esterase Antarctic HSL family GESAG motif Microbiology QR1-502 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 <i>Pseudomonas</i> sp. E2-15
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 <i>Pseudomonas</i> 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 Ser<sup>155</sup>, Asp<sup>253</sup>, and His<sup>282</sup> residues. The catalytic efficiency (<i>k</i><sub>cat</sub>/<i>K</i><sub>m</sub>) of Est19 for the <i>p</i>NPC6 substrate is 148.68 s<sup>−1</sup>mM<sup>−1</sup> at 40 °C. Replacing Glu<sup>154</sup> 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	article
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 <i>Pseudomonas</i> sp. E2-15
title_short	Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium <i>Pseudomonas</i> sp. E2-15
title_full	Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium <i>Pseudomonas</i> sp. E2-15
title_fullStr	Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium <i>Pseudomonas</i> sp. E2-15
title_full_unstemmed	Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium <i>Pseudomonas</i> sp. E2-15
title_sort	identification and biochemical characterization of a novel hormone-sensitive lipase family esterase est19 from the antarctic bacterium <i>pseudomonas</i> sp. e2-15
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/26af0279e2d143e193f8ad781c2465ab
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Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium <i>Pseudomonas</i> sp. E2-15

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