(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 > Deuterostomia: NE > Chordata: NE > Craniata: NE > Vertebrata: NE > Gnathostomata: NE > Teleostomi: NE > Euteleostomi: NE > Actinopterygii: NE > Actinopteri: NE > Neopterygii: NE > Teleostei: NE > Osteoglossocephalai: NE > Clupeocephala: NE > Otomorpha: NE > Ostariophysi: NE > Otophysi: NE > Characiphysae: NE > Gymnotiformes: NE > Gymnotoidei: NE > Gymnotidae: NE > Electrophorus: NE > Electrophorus electricus: NE
E463R : The binding sites of inhibitory monoclonal antibodies on acetylcholinesterase. Identification of a novel regulatory site at the putative back door L280H : The binding sites of inhibitory monoclonal antibodies on acetylcholinesterase. Identification of a novel regulatory site at the putative back door L460V : The binding sites of inhibitory monoclonal antibodies on acetylcholinesterase. Identification of a novel regulatory site at the putative back door Q277H : The binding sites of inhibitory monoclonal antibodies on acetylcholinesterase. Identification of a novel regulatory site at the putative back door S74L : The binding sites of inhibitory monoclonal antibodies on acetylcholinesterase. Identification of a novel regulatory site at the putative back door WT_eleel-ACHE : Hydrolysis by acetylcholinesterase. Apparent molal volumes and trimethyl and methyl subsites
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 MKILDALLFPVIFIMFFIHLSIAQTDPELTIMTRLGQVQGTRLPVPDRSH VIAFLGIPFAEPPLGKMRFKPPEPKKPWNDVFDARDYPSACYQYVDTSYP GFSGTEMWNPNRMMSEDCLYLNVWVPATPRPHNLTVMVWIYGGGFYSGSS SLDVYDGRYLAHSEKVVVVSMNYRVSAFGFLALNGSAEAPGNVGLLDQRL ALQWVQDNIHFFGGNPKQVTIFGESAGAASVGMHLLSPDSRPKFTRAILQ SGVPNGPWRTVSFDEARRRAIKLGRLVGCPDGNDTDLIDCLRSKQPQDLI DQEWLVLPFSGLFRFSFVPVIDGVVFPDTPEAMLNSGNFKDTQILLGVNQ NEGSYFLIYGAPGFSKDNESLITREDFLQGVKMSVPHANEIGLEAVILQY TDWMDEDNPIKNREAMDDIVGDHNVVCPLQHFAKMYAQYSILQGQTGTAS QGNLGWGNSGSASNSGNSQVSVYLYMFDHRASNLVWPEWMGVIHGYEIEF VFGLPLEKRLNYTLEEEKLSRRMMKYWANFARTGNPNINVDGSIDSRRRW PVFTSTEQKHVGLNTDSLKVHKGLKSQFCALWNRFLPRLLNVTENIDDAE RQWKAEFHRWSSYMMHWKNQFDHYSKQERCTNL
References
Title: Conformational flexibility of the acetylcholinesterase tetramer suggested by x-ray crystallography Bourne Y, Grassi J, Bougis PE, Marchot P Ref: Journal of Biological Chemistry, 274:30370, 1999 : PubMed
Acetylcholinesterase, a polymorphic enzyme, appears to form amphiphilic and nonamphiphilic tetramers from a single splice variant; this suggests discrete tetrameric arrangements where the amphipathic carboxyl-terminal sequences can be either buried or exposed. Two distinct, but related crystal structures of the soluble, trypsin-released tetramer of acetylcholinesterase from Electrophorus electricus were solved at 4.5 and 4.2 A resolution by molecular replacement. Resolution at these levels is sufficient to provide substantial information on the relative orientations of the subunits within the tetramer. The two structures, which show canonical homodimers of subunits assembled through four-helix bundles, reveal discrete geometries in the assembly of the dimers to form: (a) a loose, pseudo-square planar tetramer with antiparallel alignment of the two four-helix bundles and a large space in the center where the carboxyl-terminal sequences may be buried or (b) a compact, square nonplanar tetramer that may expose all four sequences on a single side. Comparison of these two structures points to significant conformational flexibility of the tetramer about the four-helix bundle axis and along the dimer-dimer interface. Hence, in solution, several conformational states of a flexible tetrameric arrangement of acetylcholinesterase catalytic subunits may exist to accommodate discrete carboxyl-terminal sequences of variable dimensions and amphipathicity.
Title: Quaternary Structure of Tetrameric Acetylcholinesterase Raves ML, Giles K, Schrag JD, Schmid MF, Phillips JN, Jr., Chiu W, Howard AJ, Silman I, Sussman JL Ref: In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases, (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp.:351, 1998 : PubMed
Title: Cloning and expression of acetylcholinesterase from Electrophorus. Splicing pattern of the 3' exons in vivo and in transfected mammalian cells Simon S, Massoulie J Ref: Journal of Biological Chemistry, 272:33045, 1997 : PubMed
We cloned and expressed a cDNA encoding acetylcholinesterase (AChE) of type T from Electrophorus electricus organs. When expressed in COS, HEK, and Chinese hamster ovary cells, the AChET subunits generated dimers and tetramers. The cells produced more activity at 27 than at 37 degrees C. The kinetic parameters of a recombinant enzyme, produced in the yeast Pichia pastoris, were close to those of the natural AChE. Analysis of genomic clones showed that the coding sequence is interrupted by an intron that does not exist in Torpedo and differs in its location from that observed in the mouse. This intron is preceded by a sequence encoding a non-conserved 29-amino acid peptide, which does not exist in Torpedo or mammalian AChEs. According to a three-dimensional model, this non-conserved peptide is located at the surface of the protein, opposite from the entry of the catalytic gorge; its deletion did not modify the catalytic parameters. Sequence analyses and expression of various constructs showed that the gene does not contain any H exon. We also found that splicing of transcripts in mammalian cells reveals cryptic donor sites in exons and acceptor sites in introns, which do not appear to be used in vivo.
Electrophorus electricus (Electric eel) (Gymnotus electricus) acetylcholinesterase
