Unraveling the regioselectivity of Ophiostoma piceae sterol esterase as a case study for lipases with wide acyl-binding tunnel entrances
SNU CALS team led by Prof. Pahn-Shick Chang has elucidated the structural mechanism underlying the sn-1(3) regioselectivity of OPE and established a comprehensive correlation between tunnel morphology and positional preference in lipases. By integrating chiral-phase resolution and molecular dynamics simulations, the team demonstrated how the width of tunnel entrance dictates catalytic orientation, providing structural insights for the enzymatic synthesis of tailor-made structured lipids.
