Bao, R., He, L.H., Liu, B. some differences in sequence
Ligand
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Reference
Title: Protein Crystallography and Site-Direct Mutagenesis Analysis of the Poly(ethylene terephthalate) Hydrolase PETase from Ideonella sakaiensis Liu B, He L, Wang L, Li T, Li C, Liu H, Luo Y, Bao R Ref: Chembiochem, 19:1471, 2018 : PubMed
Unlike traditional recycling strategies, biodegradation is a sustainable solution for disposing of poly(ethylene terephthalate) (PET) waste. PETase, a newly identified enzyme from Ideonella sakaiensis, has high efficiency and specificity towards PET and is, thus, a prominent candidate for PET degradation. On the basis of biochemical analysis, we propose that a wide substrate-binding pocket is critical for its excellent ability to hydrolyze crystallized PET. Structure-guided site-directed mutagenesis revealed an improvement in PETase catalytic efficiency, providing valuable insight into how the molecular engineering of PETase can optimize its application in biocatalysis.
        
Representative scheme of Polyesterase-lipase-cutinase structure and an image from PDBsum server
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5YFEFold classification based on Structure-Structure alignment of Proteins - FSSP server