Structural insights into thraustochytrid-specific lipases using alphafold to identify the role of GXSXG motif

Our study provides novel insights regarding the structure and ligand binding affinities for thraustochytrid specific lipases which are diversified attributed to the heterogeneity within the catalytic triads. In conclusion, we hypothesize that differential localization and higher binding efficiency of thraustochytrid specific lipases allow the microbe to efficiently utilize oil substrates. These thraustochytrid-specific lipases are potential candidates for commercialization as large-scale production of thraustochytrids can be achieved sustainably by cultivating on sustainable substrates and these enzymes are highly efficient and robust.