Sandbox Reserved 1846: Difference between revisions

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Because cutinases are members of the α/β-hydrolase superfamily and can hydrolyze polymer esters, LCC has shown high efficiency in hydrolyzing [https://en.wikipedia.org/wiki/Polyethylene_terephthalate polyethylene terephthalate] (PET), which is a widely used plastic that contributes to pollution. Unlike many other PET-degrading enzymes, LCC has a high [https://en.wikipedia.org/wiki/Specificity_constant catalytic efficiency] ''and'' is thermostable, which means it can function at temperatures that are optimal for industrial recycling processes.<ref name="Khairul">PMID:36293501</ref><ref name="Burgin">PMID:38538850</ref> By breaking PET into its monomers, LCC promotes [https://en.wikipedia.org/wiki/Closed-loop_recycling closed-loop recycling] of plastic waste and reduces environmental accumulation.<ref name="Sui"/>

[https://www.rcsb.org/structure/4EB0 4EB0] is the primary PDB file used throughout this page. The protein is an LCC mutant that has been optimized for thermostability. The model substrate is 2-HE(MHET)₃, a trimer of MHET [https://en.wikipedia.org/wiki/2-Hydroxyethyl_terephthalic_acid (mono-(2-hydroxy-ethyl) terephthalate)]. MHET is an intermediate in the depolymerization of PET.<ref name="Zhang">PMID:37945666</ref><ref name="Tournier"/>

[https://www.rcsb.org/structure/4EB0 4EB0] is the primary PDB file used throughout this page. The protein is an LCC mutant that has been optimized for thermostability. The model substrate is 2-HE(MHET)₃, a trimer of MHET [https://en.wikipedia.org/wiki/2-Hydroxyethyl_terephthalic_acid (mono-(2-hydroxy-ethyl) terephthalate)]. MHET is an intermediate in the depolymerization of PET.<ref name="Zhang">PMID:37945666</ref><ref name="Tournier"/> A binding model of the substrate 2-HE(MHET)3 in wild-type LLC (4eb0.pdb) was constructed and refined to mimic the 3D structure illustrated in Figure 2 of reference “xx”. The software Maestro (Schrödinger, Inc; version 14.2.118) was used to construct the initial binding structure, followed by energy minimization in the context of the rigid protein that had previously been processed to add/refine all hydrogen atoms. The ligand model was then used without further modification to identify and illustrate the cited active-site residues.

== Function ==

Sandbox Reserved 1846: Difference between revisions

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 Because cutinases are members of the α/β-hydrolase superfamily and can hydrolyze polymer esters, LCC has shown high efficiency in hydrolyzing [https://en.wikipedia.org/wiki/Polyethylene_terephthalate polyethylene terephthalate] (PET), which is a widely used plastic that contributes to pollution. Unlike many other PET-degrading enzymes, LCC has a high [https://en.wikipedia.org/wiki/Specificity_constant catalytic efficiency] ''and'' is thermostable, which means it can function at temperatures that are optimal for industrial recycling processes.<ref name="Khairul">PMID:36293501</ref><ref name="Burgin">PMID:38538850</ref> By breaking PET into its monomers, LCC promotes [https://en.wikipedia.org/wiki/Closed-loop_recycling closed-loop recycling] of plastic waste and reduces environmental accumulation.<ref name="Sui"/>
-[https://www.rcsb.org/structure/4EB0 4EB0] is the primary PDB file used throughout this page. The protein is an LCC mutant that has been optimized for thermostability. The model substrate is 2-HE(MHET)₃, a trimer of MHET [https://en.wikipedia.org/wiki/2-Hydroxyethyl_terephthalic_acid (mono-(2-hydroxy-ethyl) terephthalate)]. MHET is an intermediate in the depolymerization of PET.<ref name="Zhang">PMID:37945666</ref><ref name="Tournier"/>
+[https://www.rcsb.org/structure/4EB0 4EB0] is the primary PDB file used throughout this page. The protein is an LCC mutant that has been optimized for thermostability. The model substrate is 2-HE(MHET)₃, a trimer of MHET [https://en.wikipedia.org/wiki/2-Hydroxyethyl_terephthalic_acid (mono-(2-hydroxy-ethyl) terephthalate)]. MHET is an intermediate in the depolymerization of PET.<ref name="Zhang">PMID:37945666</ref><ref name="Tournier"/> A binding model of the substrate 2-HE(MHET)3 in wild-type LLC (4eb0.pdb) was constructed and refined to mimic the 3D structure illustrated in Figure 2 of reference “xx”. The software Maestro (Schrödinger, Inc; version 14.2.118) was used to construct the initial binding structure, followed by energy minimization in the context of the rigid protein that had previously been processed to add/refine all hydrogen atoms. The ligand model was then used without further modification to identify and illustrate the cited active-site residues.
 == Function ==