A novel family VIII carboxylesterase hydrolysing third- and fourth-generation cephalosporins
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Title
- A novel family VIII carboxylesterase hydrolysing third- and fourth-generation cephalosporins
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Author(s)
- Jeon, Jeong Ho; Lee, Hyun Sook; Lee, Jung Hun; Koo, Bon-Sung; Lee, Chang-Muk; Lee, Sang Hee; Kang, Sung Gyun; Lee, Jung-Hyun
- KIOST Author(s)
- Lee, Hyun Sook(이현숙); Kang, Sung Gyun(강성균); Lee, Jung Hyun(이정현)
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Alternative Author(s)
- 이현숙; 강성균; 이정현
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Publication Year
- 2016-04
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Abstract
- A metagenomic library was constructed from a soil sample of spindle tree-rhizosphere. From this library, one clone with esterase activity was selected. The sequence analysis revealed an open reading frame (EstSTR1) encoded protein of 390 amino acids. EstSTR1 is a family VIII carboxylesterase and retains the S-X-X-K motif conserved in both family VIII carboxylesterases and class C beta-lactamases. The estSTR1 gene was overexpressed in E. coli and the recombinant protein was purified by purified by metal chelating affinity chromatography and size-exclusion chromatography. EstSTR1 hydrolysed p-nitrophenyl esters, exhibited the highest activity toward p-nitrophenyl butyrate. Furthermore, EstSTR1 could hydrolyse third-and fourth-generation cephalosporins (cefotaxime and cefepime) as well as first-generation cephalosporin (cephalothin). Site-directed mutagenesis studies revealed that a catalytic residue, Ser71, of EstSTR1 plays an essential role in hydrolysing both antibiotics and p-nitrophenyl esters. We demonstrate that a metagenome-derived carboxylesterase displays beta-lactam-hydrolysing activities toward third- and fourth-generation cephalosporins.
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ISSN
- 2193-1801
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URI
- https://sciwatch.kiost.ac.kr/handle/2020.kiost/2206
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DOI
- 10.1186/s40064-016-2172-y
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Bibliographic Citation
- SPRINGERPLUS, v.5, 2016
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Publisher
- SPRINGER INTERNATIONAL PUBLISHING AG
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Keywords
- Metagenome; beta-Lactamase; Carboxylesterase; Extended-spectrum cephalosporins
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Type
- Article
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Language
- English
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Document Type
- Article
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