Structural studies reveal the molecular mechanism of PETase

摘要: Poly(ethylene terephthalate) (PET) is a class of plastic material widely used in modern society, but large amounts PET waste cause severe environmental problems. Obtained from PET-consuming bacterium Ideonella sakaiensis, the enzyme PETase exhibits superb hydrolytic activity and substrate preference toward PET. Here, we summarize some recent advances crystallographic analysis PETase. These reports uncover structural features that are involved its catalytic activity. In comparison to homologous enzymes, contains an additional disulfide bond as well extended β8-α6 loop. More importantly, crystal structures complex with product analogs provide critical information for understanding mechanism action particular, wobbling conformation W156 closely related binding product. new findings great importance further in-depth research engineering development PETase, should advance implementation biodegradation strategy.