Peptidyl-Ser-tetrahedral intermediate (with previous acetylcholine carboxylic-ester)
Acetyl-enzyme (Peptidyl-Ser-acetyl group)
Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein.
Substrate inhibition of acetylcholinesterase: residues affecting signal transduction from the surface to the catalytic center.
1.9-A resolution structure of fasciculin 1, an anti-acetylcholinesterase toxin from green mamba snake venom.
MUTAGENESIS OF ACTIVE SITE RESIDUES AND OF ASP-206 AND ASP-435.
Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding.
Excavations into the active-site gorge of cholinesterases.
Three-dimensional structure of acetylcholinesterase and of its complexes with anticholinesterase drugs.
Engineering resistance to 'aging' of phosphylated human acetylcholinesterase. Role of hydrogen bond network in the active center.
Key active site residues in the inhibition of acetylcholinesterases by soman.
Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase.
Three-dimensional structures of acetylcholinesterase and of its complexes with anticholinesterase agents.
Molecular recognition in acetylcholinesterase catalysis: free-energy correlations for substrate turnover and inhibition by trifluoro ketone transition-state analogs.
Structure and dynamics of the active site gorge of acetylcholinesterase: synergistic use of molecular dynamics simulation and X-ray crystallography.
Open "back door" in a molecular dynamics simulation of acetylcholinesterase.
Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsite.
Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex.
Contribution of aromatic moieties of tyrosine 133 and of the anionic subsite tryptophan 86 to catalytic efficiency and allosteric modulation of acetylcholinesterase.
Allosteric control of acetylcholinesterase catalysis by fasciculin.
Theoretical analysis of the structure of the peptide fasciculin and its docking to acetylcholinesterase.
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF COMPLEX WITH FASCICULIN.
Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target.
Aging of phosphylated human acetylcholinesterase: catalytic processes mediated by aromatic and polar residues of the active centre.
Aspartate 74 as a primary determinant in acetylcholinesterase governing specificity to cationic organophosphonates.
Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function.
Structural modifications of the omega loop in human acetylcholinesterase.
The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase.
Soluble monomeric acetylcholinesterase from mouse: expression, purification, and crystallization in complex with fasciculin.
Studies on a new series of THA analogues: effects of the aromatic residues that line the gorge of AChE.
Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A.
Molecular mechanic study of nerve agent O-ethyl S-[2-(diisopropylamino)ethyl]methylphosphonothioate (VX) bound to the active site of Torpedo californica acetylcholinesterase.
Static Laue diffraction studies on acetylcholinesterase.
The 'aromatic patch' of three proximal residues in the human acetylcholinesterase active centre allows for versatile interaction modes with inhibitors.
The role of TRP84 in catalytic power and the specificity of AChE.
Three-dimensional structure of a complex of E2020 with acetylcholinesterase from Torpedo californica.
X-ray crystallography (ISBN: 0306460505)
Structure and Function of Cholinesterases and Related Proteins
Quaternary structure of tetrameric acetylcholinesterase.
"Back door" opening implied by the crystal structure of a carbamoylated acetylcholinesterase.
Phosphoryl oxime inhibition of acetylcholinesterase during oxime reactivation is prevented by edrophonium.
Crystal structures of aged phosphonylated acetylcholinesterase: nerve agent reaction products at the atomic level.
Structure of acetylcholinesterase complexed with (-)-galanthamine at 2.3 A resolution.
Reaction products of acetylcholinesterase and VX reveal a mobile histidine in the catalytic triad.
Conformational flexibility of the acetylcholinesterase tetramer suggested by x-ray crystallography.
Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly.
Predicting relative binding free energies of tacrine-huperzine A hybrids as inhibitors of acetylcholinesterase.
Structure of acetylcholinesterase complexed with E2020 (Aricept): implications for the design of new anti-Alzheimer drugs.
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 36-574.
Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II.
Mechanism of oxime reactivation of acetylcholinesterase analyzed by chirality and mutagenesis.
Docking study of enantiomeric fonofos oxon bound to the active site of Torpedo californica acetylcholinesterase.
Active-site gorge and buried water molecules in crystal structures of acetylcholinesterase from Torpedo californica.
Pathways of ligand clearance in acetylcholinesterase by multiple copy sampling.
Specific chemical and structural damage to proteins produced by synchrotron radiation.
Molecular dynamics study of active-site interactions with tetracoordinate transients in acetylcholinesterase and its mutants.
A structural motif of acetylcholinesterase that promotes amyloid beta-peptide fibril formation.
Does "butyrylization" of acetylcholinesterase through substitution of the six divergent aromatic amino acids in the active center gorge generate an enzyme mimic of butyrylcholinesterase?
Short, strong hydrogen bonds at the active site of human acetylcholinesterase: proton NMR studies.
A structure-based design approach to the development of novel, reversible AChE inhibitors.
Methyl analogues of the experimental Alzheimer drug phenserine: synthesis and structure/activity relationships for acetyl- and butyrylcholinesterase inhibitory action.
Accurate prediction of the bound conformation of galanthamine in the active site of Torpedo californica acetylcholinesterase using molecular docking.
Specific protein dynamics near the solvent glass transition assayed by radiation-induced structural changes.
Three-dimensional structure of a complex of galanthamine (Nivalin) with acetylcholinesterase from Torpedo californica: implications for the design of new anti-Alzheimer drugs.
Molecular dynamics of acetylcholinesterase.
Structure of a complex of the potent and specific inhibitor BW284C51 with Torpedo californica acetylcholinesterase.
The aromatic "trapping" of the catalytic histidine is essential for efficient catalysis in acetylcholinesterase.
Kinetic and structural studies on the interaction of cholinesterases with the anti-Alzheimer drug rivastigmine.
X-ray structures of Torpedo californica acetylcholinesterase complexed with (+)-huperzine A and (-)-huperzine B: structural evidence for an active site rearrangement.
3D structure of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 A resolution: kinetic and molecular dynamic correlates.
Substrate activation in acetylcholinesterase induced by low pH or mutation in the pi-cation subsite.
Detection of unwanted protein-bound ligands by capillary zone electrophoresis: the case of hidden ligands that stabilize cholinesterase conformation.
A neutral molecule in a cation-binding site: specific binding of a PEG-SH to acetylcholinesterase from Torpedo californica.
Unmasking tandem site interaction in human acetylcholinesterase. Substrate activation with a cationic acetanilide substrate.
Acetylcholinesterase in motion: visualizing conformational changes in crystal structures by a morphing procedure.
Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site.
Aromatic amino-acid residues at the active and peripheral anionic sites control the binding of E2020 (Aricept) to cholinesterases.
Acetylcholinesterase complexed with bivalent ligands related to huperzine A: experimental evidence for species-dependent protein-ligand complementarity.
Nanosecond dynamics of the mouse acetylcholinesterase cys69-cys96 omega loop.
Molecular docking studies of natural cholinesterase-inhibiting steroidal alkaloids from Sarcococca saligna.
Is aromaticity essential for trapping the catalytic histidine 447 in human acetylcholinesterase?
Nanosecond dynamics of acetylcholinesterase near the active center gorge.
A computational study of the binding of propidium to the peripheral anionic site of human acetylcholinesterase.
The complex of a bivalent derivative of galanthamine with torpedo acetylcholinesterase displays drastic deformation of the active-site gorge: implications for structure-based drug design.
According to the literature [1] & [24], this enzyme has got a similar catalytic triad to that of serine proteases, including trypsin (D00197 in EzCatDB), although glutamate is used instead of aspartate as a modulator. Moreover, normally two amide groups form an oxyanion hole, but this enzyme use three amide groups (from Gly118, Gly119 & Ala201) to form it for the transition-state stabilization. (Ser200 acts as a nucleophile, whereas His440 acts as a general acid-base.)