| The resistance of most insects to insecticides and adaptation to host plants can be attributed to the metabolic effects of cytochrome P450s enzymes on insecticides and other foreign substances.The protein structure and characteristics of CYP4,CYP6,CYP9 and other subfamily genes in Agasicles hygrophila cytochrome P450s enzyme system were analyzed from the perspective of bioinformatics,and their possible functions were estimated.By means of Bioinformatic method,the physicochemical properties,signal peptides,subcellular localization,transmembrane structure,secondary structure,advanced structure,multiple sequences alignment and phylogenetic tree of A.hygrophila P450s were analysized.In the laboratory’s previous work,nine of A.hygrophila P450s genes have been cloned and identified.They are named CYP347J1,CYP4FE1,CYP4G116,CYP4G117,CYP6HR1,CYP6HS1,CYP9Z53,CYP9Z54 and CYP9Z55.Including CYP3,CYP4,CYP6,CYP9 family.The full-length cDNA is between 1614bp and 1788bp,498 to 586 amino acids.The cytochrome P450s of A.hygrophila has no signal peptides,and most of the subcellular localization is cytoplasm,and generally contains a transmembrane structure.The secondary structure of A.hygrophila P450s is mainly composed of α-helices and random coils.The advanced structure consists of an alpha helix formed by disulfide bonds between two adjacent cysteine residues,maintaining a hydrophobic cavity and a hydrophilic surface.Multiple sequence alignments showed that the cytochrome P450 of A.hygrophila was consistent with the conserved domain of insect P450.Phylogenetic analysis showed that the P450 of A.hygrophila had a high similarity between intraspecific and interspecies.The cytochrome P450s protein of A.hygrophila has phosphorylation sites for serine,threonine,and tyrosine protein kinases;Glycosylation sites with serine and threonine protein kinases;Alanine protein kinase with acetylation sites.This article predicts the possible structure and function of the protein of A.hygrophila from nine P450 genes.This study lays a theoretical foundation for the further study of biological functions of A.hygrophila through the identification and analysis. |