Torpedo californica, acetylcholinesterase

The esteratic subsite contains the catalytic machinery of the enzyme. The catalytic triad residues - Ser 200, His 440 and Glu 327 (the residue numbering in this section refers to Torpedo californica acetylcholinesterase, TcAChE) - are identical in both enzymes and basically in the same positions. 

Schumacher, M. Camp, S. Maulet, Y. Newton, M. MacPhee-Quigley, K. Taylor, S. S. Friedmann, T. Taylor, P. Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence. Nature 1986, 319, 407 09. 

Dvir, H. Wong, D. M. Harel, M. Barril, X. Orozco, M. Luque, F. J. Munoz-Torrero, D. Camps, R Rosenberry, T. L. Silman, I. Sussman, J. L. 3D stmeture of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 angstrom resolution kinetic and molecular dynamic correlates. Biochemistry, 2002, 41(9) 2970-2981. 

Doom, J.A., Thompson, C.M., Christner, R.B., Richardson, R.J. (2003). Stereoselective interaction of Torpedo californica acetylcholinesterase by isomalathion inhibitory reactions with (IR)- and (lR)-isomers proceed by different mechanisms. Chem. Res. Toxicol. 16 958-65. 

BUcht, G., Haggstrom, B., Radio, Z., Ostertnan, A., and Hjalmarsson, K. (1994). Residues important for folding and dimerisatitm of recombinant Torpedo californica acetylcholinesterase. Biochim. Biophys. Acta 1209, 265-273,... 

Fig 5-2. This schematic ribbon diagram shows the structure of Torpedo californica acetylcholinesterase. The diagram is color-coded green the 537-amino acid polypeptide of the enzyme monomer pink the 14 aromatic residues that line the deep aromatic gorge leading to the active site and gold and blue a model of the natural substrate for acetylcholinesterase, the neurotransmitter acetylcholine, docked in the active site. Reprinted with permission from Sussman JL, Silman I. Acetylcholinesterase Structure and use as a model for specific cation-protein interactions. Curr Opin Struct Biol. 1992 2 724. 

Dvir H, Jiang HL, Wong DM, Harel M, Chetrit M, He XC, Jin GY, Yu GL, Tang XC, Silman I, Bai DL, Sussman JL (2002) X-ray structures of Torpedo californica acetylcholinesterase complexed with (-t)-Huperzine A and (—)-huperzine B structural evidence for an active site rearrangement. Biochemistry 41(35) 10810-10818. doi 10.1021/ bi020151-l-... 

Sussman, J.L., Harel, M., Frolow, F., Oefner, C., Goldman, A., Toker, L. and Silman, I. (1991) Atomic structure of acetylcholinesterase from Torpedo californica a prototypic acetylcholine-binding protein. Science 253, 872-879. 

Sussman, J. L., Silman, 1. Atomic Structure of Acetylcholinesterase from Torpedo Californica A Prototypic Acetylcholine-Binding Protein, Science 1991, 253, 872-879. 

Several members of a series of hybrid molecules of THA and huperzine-A (279) were more active against acetylcholinesterase than (-)-huperzine-A,but they were not as selective for the enzyme (compared with butyryl-cholinesterase) as huperzine-A (349). Molecular modeling of compounds in the series with acetylcholinesterase from Torpedo californica showed them to interact "as truly THA-huper-zine-A hybrids." However, it was noted that acetylcholinesterase from Torpedo is somewhat different from that of humans. A subsequent paper (350) reported a study of predic-... 

Koellner, G., Kryger, G., Millard, C.B., Silman, I., Sussman, J.L., and Steiner, T. 2000. Active-site gorge and buried water molecules in crystal structures of acetylcholinesterase from Torpedo californica.. Mol. Biol., 296, 713-735. 

Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L, Silman I. Atomic structure of acetylcholinesterase from Torpedo californica a prototypic acetylcholinebinding protein. Science 1991 253 872-879. 

W2. Weise, C., Kreienkamp, H. J., Raba, R., Pedak, A., Aaviksaar, A., and Hucho, F., Anionic subsites of the acetylcholinesterase from Torpedo californica Affinity labelling with the cationic reagent N,N-dimethyl-2-phenyl-aziridium. EMBO J. 9, 3885-3888 (1990). 

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