biostudies-literatureDo HMinistry of Oceans and Fisheries, KoreaNational Research Foundation of Korea Grante0280988https://www.ebi.ac.uk/biostudies/studies/S-EPMC9901739biostudies-literatureUnknown18(2)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, Phe19PloS oneCrystal structure and biochemical analysis of acetylesterase (LgEstI) from Lactococcus garvieae.PMC990173920200610, KOPRI Grant PM23030NRF-2021M1A5A1075524Shin SCDo HKim KKKim HWYoo WNam YWang YLee JHfalseCrystal 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 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, Phe192023-01-01T00:00:00Z20232026-05-29T03:34:22.217Z2025-04-06T19:10:42.262ZS-EPMC99017393674564410.1371/journal.pone.0280988