Pyrethroid Carboxylesterase PytH from Sphingobium faniae JZ-2: Structure and Catalytic Mechanism

doi:10.1128/AEM.02971-19

CORC > 上海应用物理研究所 > 中国科学院上海应用物理研究所 > 中科院上海应用物理研究所2011-2017年

	Pyrethroid Carboxylesterase PytH from Sphingobium faniae JZ-2: Structure and Catalytic Mechanism
	Xu, DQ ; Gao, YY ; Sun, B ; Ran, TT ; Zeng, LP ; He, JH ; He, J ; Wang, WW
刊名	APPLIED AND ENVIRONMENTAL MICROBIOLOGY
	2020
卷号	86 期号:12 页码:-
关键词	CRYSTAL-STRUCTURE HYDROXYNITRILE LYASE HYDROLYZING CARBOXYLESTERASE SPACE-GROUP INSECTICIDES IDENTIFICATION PURIFICATION TOXICITY ESTERASE STRAIN
ISSN号	0099-2240
DOI	10.1128/AEM.02971-19
文献子类	期刊论文
英文摘要	Carboxylesterase PytH, isolated from the pyrethroid-degrading bacterium Sphingobium faniae JZ-2, could rapidly hydrolyze the ester bond of a wide range of pyrethroid pesticides, including permethrin, fenpropathrin, cypermethrin, fenvalerate, deltamethrin, cyhalothrin, and bifenthrin. To elucidate the catalytic mechanism of PytH, we report here the crystal structures of PytH with bifenthrin (BIF) and phenylmethylsulfonyl fluoride (PMSF) and two PytH mutants. Though PytH shares low sequence identity with reported alpha/beta-hydrolase fold proteins, the typical triad catalytic center with Ser-His-Asp triad (Ser78, His230, and Asp202) is present and vital for the hydrolase activity. However, no contact was found between Ser78 and His230 in the structures we solved, which may be due to the fact that the PytH structures we determined are in their inactive or low-activity forms. The structure of PytH is composed of a core domain and a lid domain; some hydrophobic amino acid residues surrounding the substrate from both domains form a deeper and wider hydrophobic pocket than its homologous structures. This indicates that the larger hydrophobic pocket makes PytH fit for its larger substrate binding; both lid and core domains are involved in substrate binding, and the lid domain-induced core domain movement may make the active center correctly positioned with substrates. IMPORTANCE Pyrethroid pesticides are widely applied in agriculture and household; however, extensive use of these pesticides also causes serious environmental and health problems. The hydrolysis of pyrethroids by carboxylesterases is the major pathway of microbial degradation of pyrethroids, but the structure of carboxylesterases and its catalytic mechanism are still unknown. Carboxylesterase PytH from Sphingobium faniae JZ-2 could effectively hydrolyze a wide range of pyrethroid pesticides. The crystal structures of PytH are solved in this study. This showed that PytH belongs to the alpha/beta-hydrolase fold proteins with typical catalytic Ser-His-Asp triad, though PytH has a low sequence identity (about 20%) with them. The special large hydrophobic binding pocket enabled PytH to bind bigger pyrethroid family substrates. Our structures shed light on the substrate selectivity and the future application of PytH and deepen our understanding of alpha/beta-hydrolase members.
语种	英语
内容类型	期刊论文
源URL	[http://ir.sinap.ac.cn/handle/331007/33096]
专题	上海应用物理研究所_中科院上海应用物理研究所2011-2017年
作者单位	1.Nanjing Agr Univ, Key Lab Agr & Environm Microbiol, Minist Agr, Coll Life Sci, Nanjing, Peoples R China 2.Chinese Acad Sci, Shanghai Inst Appl Phys, Shanghai, Peoples R China 3.Chinese Acad Sci, Shanghai Adv Res Inst, Shanghai, Peoples R China
推荐引用方式 GB/T 7714	Xu, DQ,Gao, YY,Sun, B,et al. Pyrethroid Carboxylesterase PytH from Sphingobium faniae JZ-2: Structure and Catalytic Mechanism[J]. APPLIED AND ENVIRONMENTAL MICROBIOLOGY,2020,86(12):-.
APA	Xu, DQ.,Gao, YY.,Sun, B.,Ran, TT.,Zeng, LP.,...&Wang, WW.(2020).Pyrethroid Carboxylesterase PytH from Sphingobium faniae JZ-2: Structure and Catalytic Mechanism.APPLIED AND ENVIRONMENTAL MICROBIOLOGY,86(12),-.
MLA	Xu, DQ,et al."Pyrethroid Carboxylesterase PytH from Sphingobium faniae JZ-2: Structure and Catalytic Mechanism".APPLIED AND ENVIRONMENTAL MICROBIOLOGY 86.12(2020):-.