Characterization of a novel esterase Rv1497 of Mycobacterium tuberculosisH37Rv demonstrating β-lactamase activity.
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| Title: | Characterization of a novel esterase Rv1497 of Mycobacterium tuberculosisH37Rv demonstrating β-lactamase activity. |
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| Authors: | Singh, Gurpreet1, Kumar, Arbind1, Arya, Stuti1, Gupta, Umesh Dutt2, Singh, Kashmir1, Kaur, Jagdeep1 jagsekhon@yahoo.com |
| Source: | Enzyme & Microbial Technology. Jan2016, Vol. 82, p180-190. 11p. |
| Subjects: | Mycobacterium tuberculosis, Esterases, Beta lactamases, Serine, Enzyme activation, Penicillin |
| Abstract: | The Rv1497 (LipL) of the Mycobacterium tuberculosis H37Rv was predicted to be similar to hypothetical esterases and penicillin binding proteins of M. tuberculosis as well as to be involved in lipid metabolism. Sequence alignment revealed that Rv1497 protein contains characteristic consensus β-lactamase motif ‘SXXK’ in addition to a conserve pentapeptide –GXSXG-, characteristic of lipolytic enzymes, at the C-terminus of protein in contrast to its usual N-terminus location. For detailed characterization of protein, the rv1497 gene was cloned, expressed with N-terminal His-tag and purified to homogeneity on Ni-NTA column. Rv1497 demonstrated both esterase and β-lactamase activities. A serine located within consensus β-lactamase motif ‘SXXK’ was identified as catalytic residue in both esterase and β-lactamase enzymatic activities whereas serine residue located within conserved pentapeptide did not show any effect on both enzyme activities. The catalytic residues of Rv1497 for β-lactamase activity were determined to be Ser88, Tyr-175 and His355 residues by site-directed mutagenesis. The enzyme demonstrated preference for short chain esters (pNP-butyrate). The expression of lipL gene was significantly up-regulated during acidic stress as compared to normal conditions in in vitro culture of M. tuberculosis H37Ra. This is perhaps the first report demonstrating an esterase of mycobacterium showing β-lactamase activity. [ABSTRACT FROM AUTHOR] |
| Copyright of Enzyme & Microbial Technology is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 111498216 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Characterization of a novel esterase Rv1497 of Mycobacterium tuberculosisH37Rv demonstrating β-lactamase activity. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Singh%2C+Gurpreet%22">Singh, Gurpreet</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Kumar%2C+Arbind%22">Kumar, Arbind</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Arya%2C+Stuti%22">Arya, Stuti</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Gupta%2C+Umesh+Dutt%22">Gupta, Umesh Dutt</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Singh%2C+Kashmir%22">Singh, Kashmir</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Kaur%2C+Jagdeep%22">Kaur, Jagdeep</searchLink><relatesTo>1</relatesTo><i> jagsekhon@yahoo.com</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Enzyme+%26+Microbial+Technology%22">Enzyme & Microbial Technology</searchLink>. Jan2016, Vol. 82, p180-190. 11p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Mycobacterium+tuberculosis%22">Mycobacterium tuberculosis</searchLink><br /><searchLink fieldCode="DE" term="%22Esterases%22">Esterases</searchLink><br /><searchLink fieldCode="DE" term="%22Beta+lactamases%22">Beta lactamases</searchLink><br /><searchLink fieldCode="DE" term="%22Serine%22">Serine</searchLink><br /><searchLink fieldCode="DE" term="%22Enzyme+activation%22">Enzyme activation</searchLink><br /><searchLink fieldCode="DE" term="%22Penicillin%22">Penicillin</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: The Rv1497 (LipL) of the Mycobacterium tuberculosis H37Rv was predicted to be similar to hypothetical esterases and penicillin binding proteins of M. tuberculosis as well as to be involved in lipid metabolism. Sequence alignment revealed that Rv1497 protein contains characteristic consensus β-lactamase motif ‘SXXK’ in addition to a conserve pentapeptide –GXSXG-, characteristic of lipolytic enzymes, at the C-terminus of protein in contrast to its usual N-terminus location. For detailed characterization of protein, the rv1497 gene was cloned, expressed with N-terminal His-tag and purified to homogeneity on Ni-NTA column. Rv1497 demonstrated both esterase and β-lactamase activities. A serine located within consensus β-lactamase motif ‘SXXK’ was identified as catalytic residue in both esterase and β-lactamase enzymatic activities whereas serine residue located within conserved pentapeptide did not show any effect on both enzyme activities. The catalytic residues of Rv1497 for β-lactamase activity were determined to be Ser88, Tyr-175 and His355 residues by site-directed mutagenesis. The enzyme demonstrated preference for short chain esters (pNP-butyrate). The expression of lipL gene was significantly up-regulated during acidic stress as compared to normal conditions in in vitro culture of M. tuberculosis H37Ra. This is perhaps the first report demonstrating an esterase of mycobacterium showing β-lactamase activity. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Enzyme & Microbial Technology is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1016/j.enzmictec.2015.10.007 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 11 StartPage: 180 Subjects: – SubjectFull: Mycobacterium tuberculosis Type: general – SubjectFull: Esterases Type: general – SubjectFull: Beta lactamases Type: general – SubjectFull: Serine Type: general – SubjectFull: Enzyme activation Type: general – SubjectFull: Penicillin Type: general Titles: – TitleFull: Characterization of a novel esterase Rv1497 of Mycobacterium tuberculosisH37Rv demonstrating β-lactamase activity. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Singh, Gurpreet – PersonEntity: Name: NameFull: Kumar, Arbind – PersonEntity: Name: NameFull: Arya, Stuti – PersonEntity: Name: NameFull: Gupta, Umesh Dutt – PersonEntity: Name: NameFull: Singh, Kashmir – PersonEntity: Name: NameFull: Kaur, Jagdeep IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 01 Text: Jan2016 Type: published Y: 2016 Identifiers: – Type: issn-print Value: 01410229 Numbering: – Type: volume Value: 82 Titles: – TitleFull: Enzyme & Microbial Technology Type: main |
| ResultId | 1 |
