Paper Report for: Wang_2009_Appl.Environ.Microbiol_75_5496
Reference
Title: Cloning of a novel pyrethroid-hydrolyzing carboxylesterase gene from Sphingobium sp. strain JZ-1 and characterization of the gene product Wang BZ, Guo P, Hang BJ, Li L, He J, Li SP Ref: Applied Environmental Microbiology, 75:5496, 2009 : PubMed
A novel esterase gene, pytH, encoding a pyrethroid-hydrolyzing carboxylesterase was cloned from Sphingobium sp. strain JZ-1. The gene contained an open reading frame of 840 bp. Sequence identity searches revealed that the deduced enzyme shared the highest similarity with many alpha/beta-hydrolase fold proteins (20 to 24% identities). PytH was expressed in Escherichia coli BL21 and purified using Ni-nitrilotriacetic acid affinity chromatography. It was a monomeric structure with a molecular mass of approximately 31 kDa and a pI of 4.85. PytH was able to transform p-nitrophenyl esters of short-chain fatty acids and a wide range of pyrethroid pesticides, and isomer selectivity was not observed. No cofactors were required for enzyme activity.
Wang BZ, Guo P, Hang BJ, Li L, He J, Li SP (2009) Cloning of a novel pyrethroid-hydrolyzing carboxylesterase gene from Sphingobium sp. strain JZ-1 and characterization of the gene product Applied Environmental Microbiology75: 5496-500
Wang BZ, Guo P, Hang BJ, Li L, He J, Li SP (2009) Applied Environmental Microbiology75: 5496-500
