Sandbox Reserved 1844

This Sandbox is Reserved from March 18 through September 1, 2025 for use in the course CH462 Biochemistry II taught by R. Jeremy Johnson and Mark Macbeth at the Butler University, Indianapolis, USA. This reservation includes Sandbox Reserved 1828 through Sandbox Reserved 1846.

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Leaf Branch Compost Cutinase

spinqualitylabelsall models Protein with Ligand"<scene name= Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Text To Be Displayed</scene> Rebecca Hoff/Sandbox 1 Structural Overview Catalytic Triad As the PET substrate binds to the enzyme, its carbonyl bond attached to the first benzene ring must be harbored close to Serine in the catalytic triad (Fig. 2). Serine gets polarized by histidine, which is then stabilized by aspartic acid. Polarized Serine will attack the carbonyl bond (C-O) of the polyester, resulting in a tetrahedral in- termediate, which is then stabilized by the oxyanion hole. The hy- drolysis procedure is completed by a second nucleophilic attack mediated through a water molecule "PEThydrolase-insilico-engineering" Ligand Binding Pocket hydrophobic pocket from "An engineered PET depolymerase to break down and recycle plastic bottles" Mutation Sites of Interest S283 & D238 It gains stability with two disulfide bonds, while only one conserved disulfide bond exists in other homologs. Conserved disulfide bond C273-C289 connects the last loop to the C-terminal helix. The IsPETase-specific disulfide bond C203-C239 harbors the catalytic acid and the base [43], and has been shown to result in a lower energy barrier/higher efficiency for PET hydrolysis

Student Contributors

Ashley Callaghan Rebecca Hoff Simone McCowan