Sandbox Reserved 1844: Difference between revisions
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=Leaf Branch Compost Cutinase= | =Leaf Branch Compost Cutinase= | ||
<StructureSection load='4EB0_with_substrate.pdb' size='340' side='right' caption='Leaf Branch Compost Cutinase (PDB: 4EB0)' scene='10/1075246/4eb0_in_pink/5'> | <StructureSection load='4EB0_with_substrate.pdb' size='340' side='right' caption='Leaf Branch Compost Cutinase (PDB: 4EB0)' scene='10/1075246/4eb0_in_pink/5'> | ||
==Introduction== | ==Introduction== | ||
Leaf branch compost [https://en.wikipedia.org/wiki/Cutinase cutinase] <scene name='10/1075246/4eb0_in_pink/5'>(LCC)</scene> is a versatile enzyme that can break down both natural plant polymers and synthetic plastics.<ref name="Tournier">PMID:32269349</ref><ref name="Sui">PMID:37849919</ref> It was discovered in a [https://en.wikipedia.org/wiki/Compost compost] heap, and it originally evolved to degrade [https://en.wikipedia.org/wiki/Cutin cutin], the protective biopolymer in plant surfaces.<ref name="Ueda">PMID:34160605</ref><ref name="Kolattukudy">PMID:17779010</ref> LCC has also 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 is thermostable ''and'' has a high [https://en.wikipedia.org/wiki/Specificity_constant catalytic efficiency], 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"/> | Leaf branch compost [https://en.wikipedia.org/wiki/Cutinase cutinase] <scene name='10/1075246/4eb0_in_pink/5'>(LCC)</scene> is a versatile enzyme that can break down both natural plant polymers and synthetic plastics.<ref name="Tournier">PMID:32269349</ref><ref name="Sui">PMID:37849919</ref> It was discovered in a [https://en.wikipedia.org/wiki/Compost compost] heap, and it originally evolved to degrade [https://en.wikipedia.org/wiki/Cutin cutin], the protective biopolymer in plant surfaces.<ref name="Ueda">PMID:34160605</ref><ref name="Kolattukudy">PMID:17779010</ref> LCC has also 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 is thermostable ''and'' has a high [https://en.wikipedia.org/wiki/Specificity_constant catalytic efficiency], 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"/> | |||
== Function == | == Function == | ||
