Protein Crystallography and Site-Direct Mutagenesis Analysis of the Poly(ethylene terephthalate) Hydrolase PETase from Ideonella sakaiensis

被引：176

作者：

Liu, Bing ^{[1
,2
]}

He, Lihui ^{[2
,3
]}

Wang, Liping ^{[1
,2
]}

Li, Tao ^{[2
,3
]}

Li, Changcheng ^{[2
,3
]}

Liu, Huayi ^{[1
,2
]}

Luo, Yunzi ^{[1
,2
]}

Bao, Rui ^{[2
,3
]}

机构：

[1] Sichuan Univ, West China Hosp, Dept Gastroenterol, Chengdu 610041, Sichuan, Peoples R China

[2] Collaborat Innovat Ctr Biotherapy, Chengdu 610041, Sichuan, Peoples R China

[3] Sichuan Univ, West China Hosp, Ctr Infect Dis, Chengdu 610041, Sichuan, Peoples R China

来源：

CHEMBIOCHEM | 2018年 / 19卷 / 14期

基金：

中国国家自然科学基金;

关键词：

mutagenesis; polymers; protein engineering; sustainable chemistry; waste disposal; CUTINASE; CARBOXYLESTERASE; HYDROLYSIS; ESTERASES; PLASTICS; ENZYMES; LIPASE;

D O I：

10.1002/cbic.201800097

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：1471 / 1475

页数：5