Structural highlights
Publication Abstract from PubMedEsterase, 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. Crystal structure and biochemical analysis of acetylesterase (LgEstI) from Lactococcus garvieae.,Do H, Yoo W, Wang Y, Nam Y, Shin SC, Kim HW, Kim KK, Lee JH PLoS One. 2023 Feb 6;18(2):e0280988. doi: 10.1371/journal.pone.0280988. , eCollection 2023. PMID:36745644[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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