biostudies-literatureUnknown13Zhao JBeijing Municipal Natural Science FoundationBeijing Municipal Education CommissionNational Natural Science Foundation of ChinaFatty acid ethyl esters are important flavor chemicals in strong-flavor Baijiu. <i>Monascus purpureus</i> YJX-8 is recognized as an important microorganism for ester synthesis in the fermentation process. Enzyme LIP05 from YJX-8 can efficiently catalyze the synthesis of fatty acid ethyl esters under aqueous phase, but the key catalytic sites affecting esterification were unclear. The present work combined homology modeling, molecular dynamics simulation, molecular docking and site-directed mutation to analyze the catalytic mechanism of LIP05. Protein structure modeling indicated LIP05 belonged to α/β fold hydrolase, contained a lid domain and a core catalytic pocket with conserved catalytic triad Ser150-His215-Asp202, and the oxyanion hole composed of Gly73 and Thr74. Ile30 and Leu37 of thFrontiers in microbiology1107104https://www.ebi.ac.uk/biostudies/studies/S-EPMC9877431biostudies-literatureMolecular mechanism of LIP05 derived from <i>Monascus purpureus</i> YJX-8 for synthesizing fatty acid ethyl esters under aqueous phase.PMC9877431Dong WLiang XSun BYang MLi WZheng JLi XLu HZhao DDing ZZhang CZhao JLin MXu YfalseMolecular mechanism of LIP05 derived from <i>Monascus purpureus</i> YJX-8 for synthesizing fatty acid ethyl esters under aqueous phase.Fatty acid ethyl esters are important flavor chemicals in strong-flavor Baijiu. <i>Monascus purpureus</i> YJX-8 is recognized as an important microorganism for ester synthesis in the fermentation process. Enzyme LIP05 from YJX-8 can efficiently catalyze the synthesis of fatty acid ethyl esters under aqueous phase, but the key catalytic sites affecting esterification were unclear. The present work combined homology modeling, molecular dynamics simulation, molecular docking and site-directed mutation to analyze the catalytic mechanism of LIP05. Protein structure modeling indicated LIP05 belonged to α/β fold hydrolase, contained a lid domain and a core catalytic pocket with conserved catalytic triad Ser150-His215-Asp202, and the oxyanion hole composed of Gly73 and Thr74. Ile30 and Leu37 of th2022-01-01T00:00:00Z20222026-05-28T03:48:49.879Z2024-10-16T13:54:35.659ZS-EPMC98774313671318110.3389/fmicb.2022.1107104