Dual functional roles of a novel bifunctional beta-lactamase/esterase from Lactococcus garvieae
- Authors
- Le, Ly Thi Huong Luu; Yoo, Wanki; Wang, Ying; Jeon, Sangeun; Kim, Kyeong Kyu; Kim, Han-Woo; Kim, T. Doohun
- Issue Date
- May-2022
- Publisher
- ELSEVIER
- Keywords
- LgLacI; Bifunctional enzyme; beta-Lactamase/esterase; Antibiotics; Biodiesels
- Citation
- INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, v.206, pp 203 - 212
- Pages
- 10
- Journal Title
- INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
- Volume
- 206
- Start Page
- 203
- End Page
- 212
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/152773
- DOI
- 10.1016/j.ijbiomac.2022.02.081
- ISSN
- 0141-8130
1879-0003
- Abstract
- A novel bifunctional beta-lactamase/esterase (LgLacI), which is capable of hydrolyzing beta-lactam-containing antibiotics including ampicillin, oxacillin, and cefotaxime as well as synthesizing biodiesels, was cloned from Lactococcus garvieae. Unlike most bacterial esterases/lipases that have G-x-S-x-G motif, LgLacI, which contains S-x-x-K catalytic motif, has sequence similarities to bacterial family VIII esterase as well as beta-lactamases. The catalytic properties of LgLacI were explored using a wide range of biochemical methods including spectroscopy, assays, structural modeling, mutagenesis, and chromatography. We confirmed the bifunctional property of LgLacI hydrolyzing both esters and beta-lactam antibiotics. This study provides novel perspectives into a bifunctional enzyme from L. garvieae, which can degrade beta-lactam antibiotics with high esterase activity.
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