7qjs

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== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/PETH2_THECS PETH2_THECS] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (Ref.1). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (Ref.1, PubMed:23592055). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (Ref.1, PubMed:23592055). Capable of degrading the bioplastic poly(lactic acid) (PLLA) (PubMed:28671263).<ref>PMID:23592055</ref> <ref>PMID:28671263</ref> [UniProtKB:A0A0K8P6T7]
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[https://www.uniprot.org/uniprot/PETH1_THEFY PETH1_THEFY] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (PubMed:18658138). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:18658138, PubMed:25545638). Also hydrolyzes the triglyceride triolein (PubMed:18658138). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (PubMed:25545638).<ref>PMID:18658138</ref> <ref>PMID:25545638</ref>
== References ==
== References ==
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Current revision

Crystal structure of a cutinase enzyme from Thermobifida fusca YX (705)

PDB ID 7qjs

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