Characterization of a novel esterase Rv0045c from Mycobacterium tuberculosis.

<h4>Background</h4>It was proposed that there are at least 250 enzymes in M. tuberculosis involved in lipid metabolism. Rv0045c was predicted to be a hydrolase by amino acid sequence similarity, although its precise biochemical characterization and function remained to be defined.<h4&...

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Autores principales:	Jiubiao Guo, Xiangdong Zheng, Lipeng Xu, Zhongyuan Liu, Kehui Xu, Shentao Li, Tingyi Wen, Siguo Liu, Hai Pang
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/d269c3569a65476fa358e42c86c6ef5c
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spelling	oai:doaj.org-article:d269c3569a65476fa358e42c86c6ef5c2021-11-18T07:03:43ZCharacterization of a novel esterase Rv0045c from Mycobacterium tuberculosis.1932-620310.1371/journal.pone.0013143https://doaj.org/article/d269c3569a65476fa358e42c86c6ef5c2010-10-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20957207/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>It was proposed that there are at least 250 enzymes in M. tuberculosis involved in lipid metabolism. Rv0045c was predicted to be a hydrolase by amino acid sequence similarity, although its precise biochemical characterization and function remained to be defined.<h4>Methodology/principal findings</h4>We expressed the Rv0045c protein to high levels in E. coli and purified the protein to high purity. We confirmed that the prepared protein was the Rv0045c protein by mass spectrometry analysis. Circular dichroism spectroscopy analysis showed that the protein possessed abundant β-sheet secondary structure, and confirmed that its conformation was stable in the range pH 6.0-10.0 and at temperatures ≤ 40 °C. Enzyme activity analysis indicated that the Rv0045c protein could efficiently hydrolyze short chain p-nitrophenyl esters (C₂-C₈), and its suitable substrate was p-nitrophenyl caproate (C₆) with optimal catalytic conditions of 39 °C and pH 8.0.<h4>Conclusions/significance</h4>Our results demonstrated that the Rv0045c protein is a novel esterase. These experiments will be helpful in understanding ester/lipid metabolism related to M. tuberculosis.Jiubiao GuoXiangdong ZhengLipeng XuZhongyuan LiuKehui XuShentao LiTingyi WenSiguo LiuHai PangPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 5, Iss 10 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jiubiao Guo Xiangdong Zheng Lipeng Xu Zhongyuan Liu Kehui Xu Shentao Li Tingyi Wen Siguo Liu Hai Pang Characterization of a novel esterase Rv0045c from Mycobacterium tuberculosis.
description	<h4>Background</h4>It was proposed that there are at least 250 enzymes in M. tuberculosis involved in lipid metabolism. Rv0045c was predicted to be a hydrolase by amino acid sequence similarity, although its precise biochemical characterization and function remained to be defined.<h4>Methodology/principal findings</h4>We expressed the Rv0045c protein to high levels in E. coli and purified the protein to high purity. We confirmed that the prepared protein was the Rv0045c protein by mass spectrometry analysis. Circular dichroism spectroscopy analysis showed that the protein possessed abundant β-sheet secondary structure, and confirmed that its conformation was stable in the range pH 6.0-10.0 and at temperatures ≤ 40 °C. Enzyme activity analysis indicated that the Rv0045c protein could efficiently hydrolyze short chain p-nitrophenyl esters (C₂-C₈), and its suitable substrate was p-nitrophenyl caproate (C₆) with optimal catalytic conditions of 39 °C and pH 8.0.<h4>Conclusions/significance</h4>Our results demonstrated that the Rv0045c protein is a novel esterase. These experiments will be helpful in understanding ester/lipid metabolism related to M. tuberculosis.
format	article
author	Jiubiao Guo Xiangdong Zheng Lipeng Xu Zhongyuan Liu Kehui Xu Shentao Li Tingyi Wen Siguo Liu Hai Pang
author_facet	Jiubiao Guo Xiangdong Zheng Lipeng Xu Zhongyuan Liu Kehui Xu Shentao Li Tingyi Wen Siguo Liu Hai Pang
author_sort	Jiubiao Guo
title	Characterization of a novel esterase Rv0045c from Mycobacterium tuberculosis.
title_short	Characterization of a novel esterase Rv0045c from Mycobacterium tuberculosis.
title_full	Characterization of a novel esterase Rv0045c from Mycobacterium tuberculosis.
title_fullStr	Characterization of a novel esterase Rv0045c from Mycobacterium tuberculosis.
title_full_unstemmed	Characterization of a novel esterase Rv0045c from Mycobacterium tuberculosis.
title_sort	characterization of a novel esterase rv0045c from mycobacterium tuberculosis.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/d269c3569a65476fa358e42c86c6ef5c
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_version_	1718424008451424256

Characterization of a novel esterase Rv0045c from Mycobacterium tuberculosis.

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