(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Eukaryota: NE > Opisthokonta: NE > Metazoa: NE > Eumetazoa: NE > Bilateria: NE > Protostomia: NE > Ecdysozoa: NE > Panarthropoda: NE > Arthropoda: NE > Mandibulata: NE > Pancrustacea: NE > Hexapoda: NE > Insecta: NE > Dicondylia: NE > Pterygota: NE > Neoptera: NE > Polyneoptera: NE > Orthoptera: NE > Caelifera: NE > Acrididea: NE > Acridomorpha: NE > Acridoidea: NE > Acrididae: NE > Oedipodinae: NE > Locusta: NE > Locusta migratoria: NE > Locusta migratoria manilensis: NE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MCIFFTPPFEMAVVALGLNSRPARQVFGDFPGSVIWNPNTQLSEDCLYIN VVAPKPRPRNAAAMVWIFGGGFYSGTATLDVYDHKTLVSEENVILVSMQY RVASLGFLFFDTSDVPGNAGLFDQLMALQWVHDNIHYFGGNPHNVTLFGE SAGAVSVSIHLLSPLSRNLFSQAIMQSGSPTAPWATIDREESILRGLRLA EAVGCPHTKAEMPAVIDCLRRKNATELVNNEWGTLGICEFPFVPIIDGAI LDETPQRSLAAKNFKKTNIMMGSNTEEGYYFIIYYLTELFRKEEDVYVSR EEYLKAVRELNPYVNNVARQAIVFEYTDWANPDDPIGNRDALDKMVGDYH FTCNVNELAHRYAETGNNVYMYYFKHRSAGNPWPSWTGVMHGDEINYVFG EPLDPRKGYTPHEVELSRRMMRYWANFAKTGNPSKSEDGTWTATYWPVHT AYGREYLTLAINSSETGRGPRLKQYAFWKKYLPQLIAMTTPQPAPEPPAC VTNSTGAALQPAWGLGHRWRWGAAAQLPLAAAVALASLLRLDGTFV
References
Title: Cloning of an acetylcholinesterase gene in Locusta migratoria manilensis related to organophosphate insecticide resistance Zhou X, Xia Y Ref: Pesticide Biochemistry and Physiology, 93:77, 2009 : PubMed
An acetylcholinesterase (AChE, EC 3.1.1.7) cDNA was cloned and characterized from oriental migratory locust (Locusta migratoria manilensis). The complete cDNA contains a 1638-bp GC-rich (GC% = 66%) open reading frame encoding 546 amino acid residues. The key amino acid residues, including the three residues Ser151 (200 in Torpedo), Glu277 (327) and His391 (440) forming a catalytic triad, five out of six cysteines putatively forming intra-chain disulfide bonds, and 10 out of the 14 aromatic residues lining the active site of the Torpedo AChE, are conserved. Bioinformatics analysis shows that the cloned gene belongs to a member of ace1. RNA interfering (RNAi) with a specific double strand RNA (dsRNA) led to a significant decrease in AChE1 mRNA, enzyme synthesis and activity. Bioassay showed that the RNA interfered locust was more susceptible to malathion than the control. The results are discussed in the light of the hypothesis that the cloned AChE1 gene is related to the organophosphate insecticide resistance of L. migratoria manilensis.
        
Title: Increased activity and reduced sensitivity of acetylcholinesterase associated with malathion resistance in a field population of the oriental migratory locust, Locusta migratoria manilensis (Meyen) Yang M, Zhang J, Zhu KY, Xuan T, Liu X, Guo Y, Ma E Ref: Pesticide Biochemistry and Physiology, 91:32, 2008 : PubMed
The susceptibility to malathion, and the activity and sensitivity of acetylcholinesterase (AChE, EC 1.1.1.7) were compared between two populations of the oriental migratory locust, Locusta migratoria manilensis (Meyen) collected from Wudi County of Shandong Province in East China and Huangliu County of Hainan Province in South China. Huangliu population showed 8.5-fold resistance to malathion compared with Wudi population. AChE from Huangliu population showed 4.8-fold higher activity than that from Wudi population toward the model substrate acetylthiocholine (ATC). Kinetic studies indicated that AChE from Huangliu population had 2.6-fold lower affinity, but 5.0-fold higher catalytic activity toward ATC than AChE from Wudi population. Significantly increased activity of AChE in Huangliu population was also confirmed by non-denaturing polyacrylamide gel electrophoresis. Inhibition kinetics revealed that AChE from Huangliu population was 9.8-, 2.4-, 8.0- and 7.7-fold less sensitive to inhibition by paraoxon, malaoxon, chlopyrifos oxon, demeton-S-methyl, respectively, than that from Wudi population. Our studies revealed that a mild resistance to malathion in Huangliu population was associated with reduced sensitivity and increased catalytic activity of AChE. Our results suggest that alterations of AChE may play an important role conferring or contribute to malathion resistance in Huangliu population of the locust.