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Protein Crystallography and Site‐Direct Mutagenesis Analysis of the Poly(ethylene terephthalate) Hydrolase PETase from Ideonella sakaiensis
Author(s) -
Liu Bing,
He Lihui,
Wang Liping,
Li Tao,
Li Changcheng,
Liu Huayi,
Luo Yunzi,
Bao Rui
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800097
Subject(s) - mutagenesis , hydrolase , biocatalysis , ethylene , biodegradation , protein engineering , substrate (aquarium) , hydrolysis , chemistry , site directed mutagenesis , enzyme , active site , combinatorial chemistry , materials science , catalysis , biochemistry , organic chemistry , mutation , biology , reaction mechanism , ecology , mutant , gene
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.