Klebsiella pneumoniae ZD112 cypermethrin-degrading enzyme gene cloning and bioinformatics analysis.docVIP

 PAGE \* MERGEFORMAT 7 Klebsiella pneumoniae ZD112 cypermethrin-degrading enzyme gene cloning and bioinformatics analysis [Abstract] Objective To screen the new pyrethroid pesticide-degrading enzyme genes and understanding their characteristics, in order to solve the food and the environment to create conditions for pyrethroid pesticide residues. Methods Construction of gene library screening approach to obtain new pyrethroid pesticide-degrading enzyme (EstP) gene, and its series of bio-informatics analysis. The results gained new pyrethroid pesticide-degrading enzyme (EstP) gene. EstP are hydrolytic enzymes, encoded by 638 amino acids, predicted molecular weight of 73.4 kDa, pI value of 8.34, very low similarity with other proteins, does not belong to any known protein super-family, only to Carboxypeptidase Taq (M32) conservative domain has a certain similarity, speculated that Lys137, Glu116, Glu148 for its essential amino acid. Conclusion The new pyrethroid pesticide degradation genes to be cloned, bioinformatics analysis of its directed evolution provides a theoretical guidance for the efficient construction of genetically engineered bacteria to lay the foundation. [Keywords:] Pyrethroid pesticide-degrading enzyme; gene cloning; pyrethroid pesticides; biological information analysis Molecular cloning and bioinformatic analysis of a novel pyrethroid  hydrolyzing esterase from Klebsiella sp. Strain ZD112 WANG Zhuo  ya, LIU Yu  huan, LI He 1.Guangdong Pharmaceutical University, Guangzhou, Guangdong 510006; 2.SUN Yat  sen University, Guangzhou, Guangdong 510275, China Abstract: Objective To obtain pyrethroid  hydrolyzing esterase (EstP) gene and analyze the characteristics of it.Methods Bioinformatics analyzing tools were used to screen a EstP gene from Klebsiella sp. Strain ZD112 DNA library and predict the character and function of the protein.Results A novel EstP with higher activity was found. EstP was a protein of 638 amino acid residues,