(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 > Nematoda: NE > Chromadorea: NE > Tylenchida: NE > Aphelenchina: NE > Aphelenchoidea: NE > Aphelenchoididae: NE > Bursaphelenchus: NE > Bursaphelenchus xylophilus: 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 MSNLVELTRVAIVLWFLPRSLSRNVHHGDHLAVRTSLGVLRGVEQTYNGR RIRAFLGVPYAKKPTGSRRFSLPEMVGPWEGEMLVQEPSNTCYYTIDTMF PQFPGAEMWNPPNELSEDCLSLNIWVPEDHDGNVMVWIFGGGFVSGSPSL DLYDGRVLAVEQRSIIVNINYRLGSFGFLYFGGQSLAPGNMGLMDQQLAF KWVHHHIGSFGGDRRKVTLFGESAGGASVTSHLFAPGSADYFQRIIINSG AIINNWATKSKDVMLDMSLILAKRLNCTNQSIHRPLDDVQYILDCMRGLT AHAILREGDMVADALSLPLTFPFVPVDDDENFFKGSLIDKIKNRDFKKDL SVLLGTMKDEGTYWLPYYLSRFGFNFNHTLSSEDRHNQALISESQYRDSF EAFLPYFGGSQLVRHALMHAYERLSESEKKPERLRDGVARFVGDYFFTCS IIEFADFISDNVFDAVFMYYFTRRATSNPWPKWMGAMHGYEIEYFFGLPK RLPHLYNQEQLRIEQSFSKKIMDYWGEFSRGNPPASYWPKYNRITRKALV LSEELVTENSHHINVDVHGKQCRLIKEAEQAVRKDFYTDDLYKAQFQEET SKSGSNYNLPAIPLVVLLMILQSTL
References
Title: Inhibition of acetylcholinesterases of the pinewood nematode, Bursaphelenchus xylophilus, by phytochemicals from plant essential oils Kang JS, Kim E, Lee SH, Park IK Ref: Pesticide Biochemistry and Physiology, 105:50, 2013 : PubMed
To understand the nematicidal mode of action of phytochemicals derived from plant essential oils against the pinewood nematode (Bursaphelenchus xylophilus), we evaluated 97 compounds (49 monoterpenes, 17 phenylpropenes, 16 sesquiterpenes, and 15 sulfides) for their inhibitory effects on B. xylophilus acetylcholinesterases (BxACEs). In the primary inhibition assay using B. xylophilus crude protein, more than 50% BxACE inhibition activity was observed with 3 monoterpenes, (+)-alpha-pinene, (-)-alpha-pinene, and 3-carene; 2 phenylpropenes, omicron-anisaldehyde, and coniferyl alcohol; and 1 sesquiterpene, cis-nerolidol. Other compounds showed moderate or weak inhibitory activity. The inhibitory activities against 3 recombinant BxACEs were subsequently estimated using the identified active compounds in a primary inhibition assay. (+)-alpha-Pinene showed the strongest inhibition of BxACE-1 followed by 3-carene, coniferyl alcohol, (-)-alpha-pinene, o-anisaldehyde, and cis-nerolidol. The half maximal inhibitory concentration (IC50) values of (+)-alpha-pinene, 3-carene, o-anisaldehyde, cis-nerolidol, and (-)-alpha-pinene against BxACE-2 were found to be 0.64, 1.41, 8.18, 8.53, 15.28, and 18.03mM, respectively. Coniferyl alcohol showed the strongest inhibition of BxACE-3 followed by (+)-alpha-pinene and cis-nerolidol.
Title: Inhibition properties of three acetylcholinesterases of the pinewood nematode Bursaphelenchus xylophilus by organophosphates and carbamates Kang JS, Moon YS, Lee SH Ref: Pesticide Biochemistry and Physiology, 104:157, 2012 : PubMed
The pinewood nematode, Bursaphelenchus xylophilus, causes severe damage to pine species by transmitting the pine wilt disease, and the injection of nematicides, such as emamectin benzonate and milbemectin, is the most common practice to control this pest. However, despite their high efficacy, these macrocyclic lactone nematicides are expensive, limiting their practicability. In an attempt to screen affordable alternative nematicidal agents, we expressed three recombinant acetylcholinesterases (ACEs, EC 3.1.1.7) of B. xylophilus using an in vitro baculovirus expression system and evaluated the effects of 11 organophosphates (OPs) and three carbamates (CBs) on the toxicological properties of the enzymes. Of the three recombinant B. xylophilus ACEs (BxACEs; BxACE-1, BxACE-2 and BxACE-3), BxACE-1 and BxACE-2 were highly inhibited by OPs and CBs, including paraoxon, dichlorvos, chlorpyrifos-oxon, chlorpyrifos-methyl-oxon, mevinphos and carbofuran, as demonstrated by an inhibition assay. In contrast, BxACE-3 was insensitive to most of the pesticides tested, with the exception of mevinphos. BxACE-2 was more sensitive than BxACE-1 and BxACE-3 to most of the OPs, whereas BxACE-1 was more sensitive to the CBs than BxACE-2 and BxACE-3. An in vivo toxicity assay revealed that some compounds that were rarely employed as nematicides exhibited higher toxicities than those chemicals commonly used as nematicides. The inhibition kinetic data and in vivo toxicity assay obtained in this study should provide essential information for the development of OP- and CB-based nematicides against B. xylophilus. The availability of recombinant ACEs will also facilitate the development of an in vitro screening system to develop potential OP- and CB-based nematicides.
Title: Three acetylcholinesterases of the pinewood nematode, Bursaphelenchus xylophilus: insights into distinct physiological functions Kang JS, Lee DW, Choi JY, Je YH, Koh YH, Lee SH Ref: Molecular & Biochemical Parasitology, 175:154, 2011 : PubMed
Acetylcholinesterase (AChE) plays a key role in postsynaptic transmission in most animals. Nematodes encode multiple AChEs, implying its functional diversity. To explore physiological functions of multiple AChEs, three distinct AChEs (BxACE-1, BxACE-2, and BxACE-3) were identified and characterized from the pinewood nematode. Sequencing comparison with Torpedo AChE and Caenorhabditis elegans ACEs identified choline-binding site, catalytic triad functional site, three internal disulfide bonds and aromatic residues for the catalytic gorge. Transcriptional profiling by quantitative real-time PCR revealed that BxACE-3 is more actively transcribed than BxACE-1 (2-3 times) and BxACE-2 (9-18 times) in both propagative and dispersal stages. The three BxACEs were functionally expressed using baculovirus system. Kinetic analysis of in vitro-expressed BxACEs revealed that the substrate specificity was highest in BxACE-1 whereas the catalytic efficiency was highest in BxACE-2. In inhibition assay, BxACE-3 showed the lowest inhibition rate. Taken together, it appears that both BxACE-1 and BxACE-2 play common but non-overlapping roles in synaptic transmission, whereas BxACE-3 may have non-neuronal functions. The current findings should provide valuable insights into the evolutionary process and various physiological roles of AChE.
