Crystal structure and biochemical analysis of acetylesterase (LgEstI) from Lactococcus garvieae.
Esterase, a member of the serine hydrolase family, catalyzes the cleavage and formation of ester bonds with high regio- and stereospecificity, making them attractive biocatalysts for the synthesis of optically pure molecules. In this study, we performed an in-depth biochemical and structural charact...
| Main Authors: | , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2023-01-01
|
| Series: | PLoS ONE |
| Online Access: | https://doi.org/10.1371/journal.pone.0280988 |
| _version_ | 1797850473733029888 |
|---|---|
| author | Hackwon Do Wanki Yoo Ying Wang Yewon Nam Seung Chul Shin Han-Woo Kim Kyeong Kyu Kim Jun Hyuck Lee |
| author_facet | Hackwon Do Wanki Yoo Ying Wang Yewon Nam Seung Chul Shin Han-Woo Kim Kyeong Kyu Kim Jun Hyuck Lee |
| author_sort | Hackwon Do |
| collection | DOAJ |
| description | Esterase, a member of the serine hydrolase family, catalyzes the cleavage and formation of ester bonds with high regio- and stereospecificity, making them attractive biocatalysts for the synthesis of optically pure molecules. In this study, we performed an in-depth biochemical and structural characterization of a novel microbial acetylesterase, LgEstI, from the bacterial fish pathogen Lactococcus garvieae. The dimeric LgEstI displayed substrate preference for the short acyl chain of p-nitrophenyl esters and exhibited increased activity with F207A mutation. Comparative analysis with other esterases indicated that LgEstI has a narrow and shallow active site that may exhibit substrate specificity to short acyl chains. Unlike other esterases, LgEstI contains bulky residues such as Trp89, Phe194, and Trp217, which block the acyl chain channel. Furthermore, immobilized LgEstI retained approximately 90% of its initial activity, indicating its potential in industrial applications. This study expands our understanding of LgEstI and proposes novel ideas for improving its catalytic efficiency and substrate specificity for various applications. |
| first_indexed | 2024-04-09T19:00:51Z |
| format | Article |
| id | doaj.art-f48337076b5d49a3b1927db9b2c6f2b6 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-04-09T19:00:51Z |
| publishDate | 2023-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-f48337076b5d49a3b1927db9b2c6f2b62023-04-08T05:32:29ZengPublic Library of Science (PLoS)PLoS ONE1932-62032023-01-01182e028098810.1371/journal.pone.0280988Crystal structure and biochemical analysis of acetylesterase (LgEstI) from Lactococcus garvieae.Hackwon DoWanki YooYing WangYewon NamSeung Chul ShinHan-Woo KimKyeong Kyu KimJun Hyuck LeeEsterase, a member of the serine hydrolase family, catalyzes the cleavage and formation of ester bonds with high regio- and stereospecificity, making them attractive biocatalysts for the synthesis of optically pure molecules. In this study, we performed an in-depth biochemical and structural characterization of a novel microbial acetylesterase, LgEstI, from the bacterial fish pathogen Lactococcus garvieae. The dimeric LgEstI displayed substrate preference for the short acyl chain of p-nitrophenyl esters and exhibited increased activity with F207A mutation. Comparative analysis with other esterases indicated that LgEstI has a narrow and shallow active site that may exhibit substrate specificity to short acyl chains. Unlike other esterases, LgEstI contains bulky residues such as Trp89, Phe194, and Trp217, which block the acyl chain channel. Furthermore, immobilized LgEstI retained approximately 90% of its initial activity, indicating its potential in industrial applications. This study expands our understanding of LgEstI and proposes novel ideas for improving its catalytic efficiency and substrate specificity for various applications.https://doi.org/10.1371/journal.pone.0280988 |
| spellingShingle | Hackwon Do Wanki Yoo Ying Wang Yewon Nam Seung Chul Shin Han-Woo Kim Kyeong Kyu Kim Jun Hyuck Lee Crystal structure and biochemical analysis of acetylesterase (LgEstI) from Lactococcus garvieae. PLoS ONE |
| title | Crystal structure and biochemical analysis of acetylesterase (LgEstI) from Lactococcus garvieae. |
| title_full | Crystal structure and biochemical analysis of acetylesterase (LgEstI) from Lactococcus garvieae. |
| title_fullStr | Crystal structure and biochemical analysis of acetylesterase (LgEstI) from Lactococcus garvieae. |
| title_full_unstemmed | Crystal structure and biochemical analysis of acetylesterase (LgEstI) from Lactococcus garvieae. |
| title_short | Crystal structure and biochemical analysis of acetylesterase (LgEstI) from Lactococcus garvieae. |
| title_sort | crystal structure and biochemical analysis of acetylesterase lgesti from lactococcus garvieae |
| url | https://doi.org/10.1371/journal.pone.0280988 |
| work_keys_str_mv | AT hackwondo crystalstructureandbiochemicalanalysisofacetylesteraselgestifromlactococcusgarvieae AT wankiyoo crystalstructureandbiochemicalanalysisofacetylesteraselgestifromlactococcusgarvieae AT yingwang crystalstructureandbiochemicalanalysisofacetylesteraselgestifromlactococcusgarvieae AT yewonnam crystalstructureandbiochemicalanalysisofacetylesteraselgestifromlactococcusgarvieae AT seungchulshin crystalstructureandbiochemicalanalysisofacetylesteraselgestifromlactococcusgarvieae AT hanwookim crystalstructureandbiochemicalanalysisofacetylesteraselgestifromlactococcusgarvieae AT kyeongkyukim crystalstructureandbiochemicalanalysisofacetylesteraselgestifromlactococcusgarvieae AT junhyucklee crystalstructureandbiochemicalanalysisofacetylesteraselgestifromlactococcusgarvieae |