Unraveling the regioselectivity of Ophiostoma piceae sterol esterase as a case study for lipases with wide acyl-binding tunnel entrances.

Juno Lee, Yoonseok Choi, Taehyeong Kim, Jihoon Kim, Pahn-Shick Chang

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Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 authors.

Juno LeeResearch Institute of Agriculture and Life Sciences, Seoul National University, Seoul, Republic of Korea; Institute of Convergence Science & Technology, The Catholic University of Korea, Bucheon, Republic of Korea.

Yoonseok ChoiResearch Institute of Agriculture and Life Sciences, Seoul National University, Seoul, Republic of Korea.

Taehyeong KimResearch Institute of Agriculture and Life Sciences, Seoul National University, Seoul, Republic of Korea; Department of Biosystems Engineering, Seoul National University, Seoul, Republic of Korea; Integrated Major in Global Smart Farm, Seoul National University, Seoul, Republic of Korea.

Jihoon KimDepartment of Agricultural Biotechnology, Seoul National University, Seoul, Republic of Korea.

Pahn-Shick ChangResearch Institute of Agriculture and Life Sciences, Seoul National University, Seoul, Republic of Korea; Department of Agricultural Biotechnology, Seoul National University, Seoul, Republic of Korea; Center for Agricultural Microorganism and Enzyme, Seoul National University, Seoul, Republic of Korea; Center for Food and Bioconvergence, Seoul National University, Seoul, Republic of Korea. Electronic address: pschang@snu.ac.kr.

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6 · The paper itself

Abstract

Lipase regioselectivity (sn-1(3) vs sn-2) is crucial for synthesizing structured lipids, but the structural basis for contrasting regioselectivities in lipases with acyl-binding tunnel remains incomplete. While the correlation between a narrow tunnel entrance and sn-2 regioselectivity has been previously established, the regioselectivity of Ophiostoma piceae sterol esterase (OPE), a lipolytic enzyme with a uniquely wide tunnel entrance, remained unclear. In this study, the chiral-phase resolution of oleic species confirmed that OPE exhibits a notable sn-1(3) regioselectivity (85.8%) against trioleoylglycerol (TOG), in contrast to Candida antarctica lipase A, which possesses narrow tunnel entrance (sn-2 regioselectivity: 79.8%). Molecular dynamics simulation showed that the wide tunnel entrance of OPE facilitates stable interaction of the scissile ester group within the catalytic center only when adopting sn-1(3) binding mode; the additional C1(3)-C2 glycerol backbone linkage within TAG allows non-scissile chains to stably reside within the tunnel entrance without disrupting the interactions at the catalytic center. Overall, the results indicated that the tunnel architecture directly dictates the sn-1(3) regioselectivity of OPE, providing structural insights into the tunnel morphology-regioselectivity relationship for lipases with acyl-binding tunnel.

Indexed as

LipaseOphiostomaSterol EsteraseBinding SitesMolecular Dynamics SimulationStereoisomerismSubstrate SpecificityLipaseSterol Esteraseacyl-binding tunnelCandida antarctica lipase A (CALA)Ophiostoma piceae sterol esterase (OPE)regioselectivity

Identifiers

PMID41651420

DOI10.1016/j.jbc.2026.111230

PMCPMC12962164

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