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Cover Feature: Protein Crystallography and Site‐Direct Mutagenesis Analysis of the Poly(ethylene terephthalate) Hydrolase PETase from Ideonella sakaiensis (ChemBioChem 14/2018)
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.201800330
Subject(s) - cutinase , lipase , hydrolase , esterase , mutagenesis , enzyme , chemistry , active site , ethylene , site directed mutagenesis , cover (algebra) , biocatalysis , stereochemistry , biochemistry , catalysis , mutation , reaction mechanism , engineering , mechanical engineering , mutant , gene
The cover feature picture shows that PETase, a newly discovered enzyme from Ideonella sakaiensis , has high efficiency and specificity towards PET plastics compared to other similar enzymes (such as cutinase, esterase, or lipase). We have analyzed its crystal structure and improved its catalytic efficiency through site mutagenesis. The results suggest that this enzyme has valuable potential for further study and applications. More information can be found in the communication by Y. Luo, R. Bao, et al. on page 1471 in Issue 14, 2018 (DOI: 10.1002/cbic.201800097).