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...

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Bibliographic Details
Published in:PloS one 2023-02, Vol.18 (2), p.e0280988-e0280988
Main Authors: Do, Hackwon, Yoo, Wanki, Wang, Ying, Nam, Yewon, Shin, Seung Chul, Kim, Han-Woo, Kim, Kyeong Kyu, Lee, Jun Hyuck
Format: Article
Language:English
Subjects:
Acetylesterase
Acetylesterase - metabolism
Biocatalysts
Biochemical analysis
Biology and Life Sciences
Catalysis
Catalytic Domain
Cell culture
Chains
Chemical properties
Chemical research
Chemical synthesis
Chromatography
Cloning
Comparative analysis
Crystal structure
Crystals
Data collection
Enzymes
Esterases
Esterases - metabolism
Esters
Hydrolases
Industrial applications
Lactococcus
Lactococcus - genetics
Lactococcus garvieae
Microbial enzymes
Microorganisms
Mutagenesis
Mutation
Physical Sciences
Physiological aspects
Polyethylene terephthalate
Protein expression
Proteins
Research and Analysis Methods
Serine hydrolase
Stereospecificity
Structural analysis
Structure
Substrate preferences
Substrate Specificity
Substrates
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Summary: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.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0280988