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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LCC Crystalized Structure of Leaf-branch compost cutinase

spinqualitylabelsall models Original Structure of LCC Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. Introduction F 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" Catalytic Triad Location Ligand Binding Site hydrophobic pocket from "An engineered PET depolymerase to break down and recycle plastic bottles" Figure 1 Mutations F243 TextToBeDisplayed F243W 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 - "PEThydrolase-insilico-engineering" Key residues that were on the metal site of known homolog enzymes were identified as D238 and S283. They mutated by cysteine to introduce a disulfide bonding to increase melting temperature instead of metal ion stabilization. The engineered LCC version named LCC-ICCG (with D238C/S283C along with F243I and Y127G) is reported to acieve 90% of PET depoly- merization. Recent study by Zeng and coworkers reported an in- crease in the melting temperature of LCC-ICCG to 98.9 °C by addition of A59K, V63I, and N248P mutations. However, the optimal hydro- lyzing temperature was found to be 74 °C [58]. -"PEThydrolase-insilico-engineering"

Student Contributors

Ashley Callaghan Rebecca Hoff Simone McCowan