Le Ly Thi Huong Luu, Yoo Wanki, Wang Ying, Jeon Sangeun, Kim Kyeong Kyu, Kim Han-Woo, Kim T Doohun
Department of Chemistry, Graduate School of General Studies, Sookmyung Women's University, Seoul 04310, Republic of Korea.
Department of Chemistry, Graduate School of General Studies, Sookmyung Women's University, Seoul 04310, Republic of Korea; Department of Precision Medicine, Sungkyunkwan University, College of Medicine, Suwon 2066, Republic of Korea.
Int J Biol Macromol. 2022 May 1;206:203-212. doi: 10.1016/j.ijbiomac.2022.02.081. Epub 2022 Feb 17.
A novel bifunctional β-lactamase/esterase (LgLacI), which is capable of hydrolyzing β-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 β-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 β-lactam antibiotics. This study provides novel perspectives into a bifunctional enzyme from L. garvieae, which can degrade β-lactam antibiotics with high esterase activity.
从加氏乳球菌中克隆出一种新型双功能β-内酰胺酶/酯酶（LgLacI），它能够水解含β-内酰胺的抗生素，包括氨苄青霉素、苯唑西林和头孢噻肟，还能合成生物柴油。与大多数具有G-x-S-x-G基序的细菌酯酶/脂肪酶不同，含有S-x-x-K催化基序的LgLacI与细菌VIII族酯酶以及β-内酰胺酶具有序列相似性。利用多种生化方法，包括光谱学、测定法、结构建模、诱变和色谱法，对LgLacI的催化特性进行了探索。我们证实了LgLacI水解酯类和β-内酰胺抗生素的双功能特性。这项研究为来自加氏乳球菌的双功能酶提供了新的视角，该酶能够以高酯酶活性降解β-内酰胺抗生素。
