DB code: S00057

RLCP classification 1.12.30000.14 : Hydrolysis
CATH domain 3.40.50.1820 : Rossmann fold Catalytic domain
E.C. 3.1.1.7
CSA 2ace
M-CSA 2ace
MACiE

CATH domain Related DB codes (homologues)
3.40.50.1820 : Rossmann fold S00544 S00344 S00517 S00525 S00526 S00720 S00723 S00724 S00725 S00919 S00374 S00345 S00347 S00348 S00346 S00350 S00352 S00353 S00355 S00356 S00358 D00189 D00210 D00539 T00253

Uniprot Enzyme Name
UniprotKB Protein name Synonyms MEROPS Pfam RefSeq
P04058 Acetylcholinesterase
AChE
EC 3.1.1.7
S09.979 (Serine)
PF00135 (COesterase)
[Graphical View]
P22303 Acetylcholinesterase
AChE
EC 3.1.1.7
S09.979 (Serine)
PF08674 (AChE_tetra)
PF00135 (COesterase)
[Graphical View]
NP_000656.1 (Protein)
NM_000665.3 (DNA/RNA sequence)
NP_056646.1 (Protein)
NM_015831.2 (DNA/RNA sequence)

KEGG enzyme name
acetylcholinesterase
true cholinesterase
choline esterase I
cholinesterase
acetylthiocholinesterase
acetylcholine hydrolase
acetyl.beta-methylcholinesterase
AcCholE

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P04058 ACES_TORCA Acetylcholine + H(2)O = choline + acetate. Isoform H form is an homodimer, the asymmetric form is a disulfide-bonded oligomer composed of a collagenic subunit (Q) and a variable number of T catalytic subunits. Isoform H: Cell membrane, Lipid-anchor, GPI- anchor. Cell junction, synapse. Isoform T: Cell membrane, Peripheral membrane protein. Cell junction, synapse. Note=Attached to the membrane through disulfide linkage with the collagenic subunit, itself bound to the membrane.
P22303 ACES_HUMAN Acetylcholine + H(2)O = choline + acetate. Interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers (By similarity). Isoform H generates GPI-anchored dimers, disulfide linked. Isoform T generates multiple structures, ranging from monomers and dimers to collagen-tailed and hydrophobic-tailed forms, in which catalytic tetramers are associated with anchoring proteins that attach them to the basal lamina or to cell membranes. In the collagen-tailed forms, isoform T subunits are associated with a specific collagen, COLQ, which triggers the formation of isoform T tetramers, from monomers and dimers. Isoform R may be monomeric. Cell junction, synapse. Secreted (By similarity). Cell membrane, Peripheral membrane protein (By similarity). Isoform T: Nucleus. Note=Only observed in apoptotic nuclei. Isoform H: Cell membrane, Lipid-anchor, GPI- anchor, Extracellular side (By similarity).

KEGG Pathways
Map code Pathways E.C.
MAP00564 Glycerophospholipid metabolism

Compound table
Substrates Products Intermediates
KEGG-id C01996 C00001 C00114 C00033 I00124 I00125 I00126
E.C.
Compound Acetylcholine H2O Choline Acetate Peptidyl-Ser-tetrahedral intermediate (with previous acetylcholine carboxylic-ester) Acetyl-enzyme (Peptidyl-Ser-acetyl group) Peptidyl-Ser-acetyl-tetrahedral-intermediate
Type amine group,carbohydrate H2O amine group,carbohydrate carboxyl group
ChEBI 15355
15377
15354
15366
PubChem 187
22247451
962
305
176
21980959
1acjA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1aclA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:DME Unbound Unbound Unbound Unbound Unbound
1amnA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Transition-state-analogue:NAF Unbound Unbound
1ax9A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:EDR Unbound Unbound Unbound Unbound
1cfjA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:_GB
1dx6A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:GNT Unbound Unbound Unbound Unbound
1e3qA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1e66A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1ea5A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1eeaA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1eveA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1fssA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gpkA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gpnA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gqrA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:SAF Unbound Unbound Intermediate-analogue:EMM Unbound
1gqsA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:SAF Unbound Unbound Unbound Unbound
1h22A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1h23A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1hbjA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:FBQ
1jjbA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1oceA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Intermediate-analogue:MF2 Unbound
1qidA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1qieA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1qifA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1qigA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1qihA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1qiiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1qijA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1qikA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1qimA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1qtiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:GNT Unbound Unbound Unbound Unbound
1somA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:VXA
1votA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1vxoA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:VXA
1vxrA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Transition-state-analogue:_VX Unbound Unbound
1w4lA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:GL8 Unbound Unbound Unbound Unbound
1w6rA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:GNT Unbound Unbound Unbound Unbound
1w75A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1w75B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1w76A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:GNT Unbound Unbound Unbound Unbound
1w76B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:GNT Unbound Unbound Unbound Unbound
2aceA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Transition-state-bound:ACH Unbound Unbound
2ackA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:EDR Unbound Unbound Unbound Unbound
2dfpA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:MIS
1b41A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1f8uA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1acj & Swiss-prot;P22303, P04058

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1acjA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1aclA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1amnA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1ax9A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1cfjA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1dx6A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1e3qA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1e66A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1ea5A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1eeaA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1eveA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1fssA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1gpkA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1gpnA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1gqrA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1gqsA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1h22A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1h23A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1hbjA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1jjbA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1oceA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1qidA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1qieA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1qifA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1qigA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1qihA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1qiiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1qijA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1qikA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1qimA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1qtiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1somA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1votA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1vxoA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1vxrA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1w4lA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1w6rA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1w75A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1w75B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1w76A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
1w76B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
2aceA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
2ackA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 200;GLU 327;HIS 440 GLY 118;GLY 119;ALA 201
2dfpA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;GLU 327;HIS 440 MIS 200 GLY 118;GLY 119;ALA 201 Modified Ser200
1b41A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 203;GLU 334;HIS 447 GLY 121;GLY 122;ALA 204
1f8uA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 203;GLU 334;HIS 447 GLY 121;GLY 122;ALA 204

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
p.876-877
[8]
Scheme 1
[20]
p.838-839
[24]
p.2324-2326
[36]
Scheme 1
[52]
Scheme 1, p.5683
[53]
Fig.3

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Medline ID 91343928
PubMed ID 1678899
Journal Science
Year 1991
Volume 253
Pages 872-9
Authors Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L, Silman I
Title Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein.
Related PDB
Related UniProtKB P04058
[2]
Resource
Comments
Medline ID
PubMed ID 1396557
Journal EMBO J
Year 1992
Volume 11
Pages 3561-8
Authors Shafferman A, Velan B, Ordentlich A, Kronman C, Grosfeld H, Leitner M, Flashner Y, Cohen S, Barak D, Ariel N
Title Substrate inhibition of acetylcholinesterase: residues affecting signal transduction from the surface to the catalytic center.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 1429564
Journal J Biol Chem
Year 1992
Volume 267
Pages 22122-30
Authors le Du MH, Marchot P, Bougis PE, Fontecilla-Camps JC
Title 1.9-A resolution structure of fasciculin 1, an anti-acetylcholinesterase toxin from green mamba snake venom.
Related PDB
Related UniProtKB
[4]
Resource
Comments MUTAGENESIS OF ACTIVE SITE RESIDUES AND OF ASP-206 AND ASP-435.
Medline ID 92388112
PubMed ID 1517212
Journal J Biol Chem
Year 1992
Volume 267
Pages 17640-8
Authors Shafferman A, Kronman C, Flashner Y, Leitner M, Grosfeld H, Ordentlich A, Gozes Y, Cohen S, Ariel N, Barak D, et al
Title Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding.
Related PDB
Related UniProtKB P22303
[5]
Resource
Comments
Medline ID
PubMed ID 1412713
Journal Trends Biochem Sci
Year 1992
Volume 17
Pages 353-8
Authors Soreq H, Gnatt A, Loewenstein Y, Neville LF
Title Excavations into the active-site gorge of cholinesterases.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 8343975
Journal Chem Biol Interact
Year 1993
Volume 87
Pages 187-97
Authors Sussman JL, Harel M, Silman I
Title Three-dimensional structure of acetylcholinesterase and of its complexes with anticholinesterase drugs.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 8224249
Journal FEBS Lett
Year 1993
Volume 334
Pages 215-20
Authors Ordentlich A, Kronman C, Barak D, Stein D, Ariel N, Marcus D, Velan B, Shafferman A
Title Engineering resistance to 'aging' of phosphylated human acetylcholinesterase. Role of hydrogen bond network in the active center.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 8262242
Journal FEBS Lett
Year 1993
Volume 336
Pages 263-6
Authors Qian N, Kovach IM
Title Key active site residues in the inhibition of acetylcholinesterases by soman.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8415649
Journal Proc Natl Acad Sci U S A
Year 1993
Volume 90
Pages 9031-5
Authors Harel M, Schalk I, Ehret-Sabatier L, Bouet F, Goeldner M, Hirth C, Axelsen PH, Silman I, Sussman JL
Title Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase.
Related PDB 1acj 1acl
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 7821677
Journal Biochem Soc Trans
Year 1994
Volume 22
Pages 745-9
Authors Silman I, Harel M, Axelsen P, Raves M, Sussman JL
Title Three-dimensional structures of acetylcholinesterase and of its complexes with anticholinesterase agents.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 8031791
Journal Biochemistry
Year 1994
Volume 33
Pages 8566-76
Authors Nair HK, Seravalli J, Arbuckle T, Quinn DM
Title Molecular recognition in acetylcholinesterase catalysis: free-energy correlations for substrate turnover and inhibition by trifluoro ketone transition-state analogs.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 8003956
Journal Protein Sci
Year 1994
Volume 3
Pages 188-97
Authors Axelsen PH, Harel M, Silman I, Sussman JL
Title Structure and dynamics of the active site gorge of acetylcholinesterase: synergistic use of molecular dynamics simulation and X-ray crystallography.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 8122110
Journal Science
Year 1994
Volume 263
Pages 1276-8
Authors Gilson MK, Straatsma TP, McCammon JA, Ripoll DR, Faerman CH, Axelsen PH, Silman I, Sussman JL
Title Open "back door" in a molecular dynamics simulation of acetylcholinesterase.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 7492545
Journal Biochemistry
Year 1995
Volume 34
Pages 15444-52
Authors Barak D, Ordentlich A, Bromberg A, Kronman C, Marcus D, Lazar A, Ariel N, Velan B, Shafferman A
Title Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsite.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 8521480
Journal Cell
Year 1995
Volume 83
Pages 503-12
Authors Bourne Y, Taylor P, Marchot P
Title Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 7836436
Journal J Biol Chem
Year 1995
Volume 270
Pages 2082-91
Authors Ordentlich A, Barak D, Kronman C, Ariel N, Segall Y, Velan B, Shafferman A
Title Contribution of aromatic moieties of tyrosine 133 and of the anionic subsite tryptophan 86 to catalytic efficiency and allosteric modulation of acetylcholinesterase.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 7657613
Journal J Biol Chem
Year 1995
Volume 270
Pages 20391-9
Authors Radic Z, Quinn DM, Vellom DC, Camp S, Taylor P
Title Allosteric control of acetylcholinesterase catalysis by fasciculin.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 7613468
Journal Protein Sci
Year 1995
Volume 4
Pages 703-15
Authors van den Born HK, Radic Z, Marchot P, Taylor P, Tsigelny I
Title Theoretical analysis of the structure of the peptide fasciculin and its docking to acetylcholinesterase.
Related PDB
Related UniProtKB
[19]
Resource
Comments X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF COMPLEX WITH FASCICULIN.
Medline ID 96363673
PubMed ID 8747462
Journal Structure
Year 1995
Volume 3
Pages 1355-66
Authors Harel M, Kleywegt GJ, Ravelli RB, Silman I, Sussman JL
Title Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target.
Related PDB 1fss
Related UniProtKB P04058
[20]
Resource
Comments
Medline ID
PubMed ID 8836126
Journal Biochem J
Year 1996
Volume 318
Pages 833-40
Authors Shafferman A, Ordentlich A, Barak D, Stein D, Ariel N, Velan B
Title Aging of phosphylated human acetylcholinesterase: catalytic processes mediated by aromatic and polar residues of the active centre.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 8718893
Journal Biochemistry
Year 1996
Volume 35
Pages 10995-1004
Authors Hosea NA, Radic Z, Tsigelny I, Berman HA, Quinn DM, Taylor P
Title Aspartate 74 as a primary determinant in acetylcholinesterase governing specificity to cationic organophosphonates.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 8635606
Journal FEBS Lett
Year 1996
Volume 386
Pages 65-71
Authors Faerman C, Ripoll D, Bon S, Le Feuvre Y, Morel N, Massoulie J, Sussman JL, Silman I
Title Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 8849682
Journal FEBS Lett
Year 1996
Volume 395
Pages 22-8
Authors Velan B, Barak D, Ariel N, Leitner M, Bino T, Ordentlich A, Shafferman A
Title Structural modifications of the omega loop in human acetylcholinesterase.
Related PDB
Related UniProtKB
[24]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID
Journal J Am Chem Soc
Year 1996
Volume 118
Pages 2340-6
Authors Harel M, Quinn DM, Nair HK, Silman I, Sussman JL
Title The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase.
Related PDB 1amn
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 8845756
Journal Protein Sci
Year 1996
Volume 5
Pages 672-9
Authors Marchot P, Ravelli RB, Raves ML, Bourne Y, Vellom DC, Kanter J, Camp S, Sussman JL, Taylor P
Title Soluble monomeric acetylcholinesterase from mouse: expression, purification, and crystallization in complex with fasciculin.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 9202137
Journal FEBS Lett
Year 1997
Volume 409
Pages 155-60
Authors Pomponi M, Marta M, Colella A, Sacchi S, Patamia M, Gatta F, Capone F, Oliverio A, Pavone F
Title Studies on a new series of THA analogues: effects of the aromatic residues that line the gorge of AChE.
Related PDB
Related UniProtKB
[27]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID 97143314
PubMed ID 8989325
Journal Nat Struct Biol
Year 1997
Volume 4
Pages 57-63
Authors Raves ML, Harel M, Pang YP, Silman I, Kozikowski AP, Sussman JL
Title Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A.
Related PDB 1vot 2ace
Related UniProtKB P04058
[28]
Resource
Comments
Medline ID
PubMed ID 9261870
Journal Proteins
Year 1997
Volume 28
Pages 543-55
Authors Albaret C, Lacoutiere S, Ashman WP, Froment D, Fortier PL
Title Molecular mechanic study of nerve agent O-ethyl S-[2-(diisopropylamino)ethyl]methylphosphonothioate (VX) bound to the active site of Torpedo californica acetylcholinesterase.
Related PDB
Related UniProtKB
[29]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10089512
Journal Acta Crystallogr D Biol Crystallogr
Year 1998
Volume 54
Pages 1359-66
Authors Ravelli RB, Raves ML, Ren Z, Bourgeois D, Roth M, Kroon J, Silman I, Sussman JL
Title Static Laue diffraction studies on acetylcholinesterase.
Related PDB 1ax9
Related UniProtKB
[30]
Resource
Comments
Medline ID
PubMed ID 9742217
Journal Biochem J
Year 1998
Volume 335
Pages 95-102
Authors Ariel N, Ordentlich A, Barak D, Bino T, Velan B, Shafferman A
Title The 'aromatic patch' of three proximal residues in the human acetylcholinesterase active centre allows for versatile interaction modes with inhibitors.
Related PDB
Related UniProtKB
[31]
Resource
Comments
Medline ID
PubMed ID 9691268
Journal Biophys Chem
Year 1998
Volume 72
Pages 239-46
Authors Pomponi M, Sacchi S, Colella A, Patamia M, Marta M
Title The role of TRP84 in catalytic power and the specificity of AChE.
Related PDB
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 9789806
Journal J Physiol Paris
Year 1998
Volume 92
Pages 191-4
Authors Kryger G, Silman I, Sussman JL
Title Three-dimensional structure of a complex of E2020 with acetylcholinesterase from Torpedo californica.
Related PDB
Related UniProtKB
[33]
Resource
Comments X-ray crystallography (ISBN: 0306460505)
Medline ID
PubMed ID
Journal Structure and Function of Cholinesterases and Related Proteins
Year 1998
Volume
Pages
Authors Raves ML, Giles K, Schrag JD, Schmid MF, Phillips GN, Wah C, Howard AJ, Silman I, Sussman JL
Title Quaternary structure of tetrameric acetylcholinesterase.
Related PDB 1eea
Related UniProtKB
[34]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
Medline ID 99249780
PubMed ID 10231521
Journal Biochemistry
Year 1999
Volume 38
Pages 5714-9
Authors Bartolucci C, Perola E, Cellai L, Brufani M, Lamba D
Title "Back door" opening implied by the crystal structure of a carbamoylated acetylcholinesterase.
Related PDB 1oce
Related UniProtKB P04058
[35]
Resource
Comments
Medline ID
PubMed ID 10433700
Journal Biochemistry
Year 1999
Volume 38
Pages 9937-47
Authors Luo C, Saxena A, Smith M, Garcia G, Radic Z, Taylor P, Doctor BP
Title Phosphoryl oxime inhibition of acetylcholinesterase during oxime reactivation is prevented by edrophonium.
Related PDB
Related UniProtKB
[36]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID 99282167
PubMed ID 10353814
Journal Biochemistry
Year 1999
Volume 38
Pages 7032-9
Authors Millard CB, Kryger G, Ordentlich A, Greenblatt HM, Harel M, Raves ML, Segall Y, Barak D, Shafferman A, Silman I, Sussman JL
Title Crystal structures of aged phosphonylated acetylcholinesterase: nerve agent reaction products at the atomic level.
Related PDB 1cfj 1som 2dfp
Related UniProtKB P04058
[37]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID 20074924
PubMed ID 10606746
Journal FEBS Lett
Year 1999
Volume 463
Pages 321-6
Authors Greenblatt HM, Kryger G, Lewis T, Silman I, Sussman JL
Title Structure of acetylcholinesterase complexed with (-)-galanthamine at 2.3 A resolution.
Related PDB 1dx6
Related UniProtKB P04058
[38]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID
Journal J Am Chem Soc
Year 1999
Volume 121
Pages 9883-4
Authors Millard CB, Koellner G, Ordentlich A, Shafferman A, Silman I, Sussman JL
Title Reaction products of acetylcholinesterase and VX reveal a mobile histidine in the catalytic triad.
Related PDB 1vxo 1vxr
Related UniProtKB
[39]
Resource
Comments
Medline ID
PubMed ID 10521413
Journal J Biol Chem
Year 1999
Volume 274
Pages 30370-6
Authors Bourne Y, Grassi J, Bougis PE, Marchot P
Title Conformational flexibility of the acetylcholinesterase tetramer suggested by x-ray crystallography.
Related PDB
Related UniProtKB P04058
[40]
Resource
Comments
Medline ID
PubMed ID 9915834
Journal J Biol Chem
Year 1999
Volume 274
Pages 2963-70
Authors Bourne Y, Taylor P, Bougis PE, Marchot P
Title Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly.
Related PDB
Related UniProtKB
[41]
Resource
Comments
Medline ID
PubMed ID 10602696
Journal J Med Chem
Year 1999
Volume 42
Pages 5110-9
Authors Barril X, Orozco M, Luque FJ
Title Predicting relative binding free energies of tacrine-huperzine A hybrids as inhibitors of acetylcholinesterase.
Related PDB
Related UniProtKB
[42]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID 99197295
PubMed ID 10368299
Journal Structure Fold Des
Year 1999
Volume 7
Pages 297-307
Authors Kryger G, Silman I, Sussman JL
Title Structure of acetylcholinesterase complexed with E2020 (Aricept): implications for the design of new anti-Alzheimer drugs.
Related PDB 1eve
Related UniProtKB P04058
[43]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 36-574.
Medline ID 20508217
PubMed ID 11053835
Journal Acta Crystallogr D Biol Crystallogr
Year 2000
Volume 56
Pages 1385-94
Authors Kryger G, Harel M, Giles K, Toker L, Velan B, Lazar A, Kronman C, Barak D, Ariel N, Shafferman A, Silman I, Sussman JL
Title Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II.
Related PDB 1b41 1f8u
Related UniProtKB P22303
[44]
Resource
Comments
Medline ID
PubMed ID 10801325
Journal Biochemistry
Year 2000
Volume 39
Pages 5750-7
Authors Wong L, Radic Z, Bruggemann RJ, Hosea N, Berman HA, Taylor P
Title Mechanism of oxime reactivation of acetylcholinesterase analyzed by chirality and mutagenesis.
Related PDB
Related UniProtKB
[45]
Resource
Comments
Medline ID
PubMed ID 10732982
Journal Bioorg Med Chem
Year 2000
Volume 8
Pages 653-6
Authors Hirashima A, Kuwano E, Eto M
Title Docking study of enantiomeric fonofos oxon bound to the active site of Torpedo californica acetylcholinesterase.
Related PDB
Related UniProtKB
[46]
Resource
Comments
Medline ID
PubMed ID 10669619
Journal J Mol Biol
Year 2000
Volume 296
Pages 713-35
Authors Koellner G, Kryger G, Millard CB, Silman I, Sussman JL, Steiner T
Title Active-site gorge and buried water molecules in crystal structures of acetylcholinesterase from Torpedo californica.
Related PDB
Related UniProtKB
[47]
Resource
Comments
Medline ID
PubMed ID 10788331
Journal J Mol Biol
Year 2000
Volume 298
Pages 705-26
Authors Van Belle D, De Maria L, Iurcu G, Wodak SJ
Title Pathways of ligand clearance in acetylcholinesterase by multiple copy sampling.
Related PDB
Related UniProtKB
[48]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10639129
Journal Proc Natl Acad Sci U S A
Year 2000
Volume 97
Pages 623-8
Authors Weik M, Ravelli RB, Kryger G, McSweeney S, Raves ML, Harel M, Gros P, Silman I, Kroon J, Sussman JL
Title Specific chemical and structural damage to proteins produced by synchrotron radiation.
Related PDB 1qid 1qie 1qif 1qig 1qih 1qii 1qij 1qik 1qim
Related UniProtKB
[49]
Resource
Comments
Medline ID
PubMed ID 11171062
Journal Biochem J
Year 2001
Volume 353
Pages 645-53
Authors Enyedy IJ, Kovach IM, Bencsura A
Title Molecular dynamics study of active-site interactions with tetracoordinate transients in acetylcholinesterase and its mutants.
Related PDB
Related UniProtKB
[50]
Resource
Comments
Medline ID
PubMed ID 11523986
Journal Biochemistry
Year 2001
Volume 40
Pages 10447-57
Authors De Ferrari GV, Canales MA, Shin I, Weiner LM, Silman I, Inestrosa NC
Title A structural motif of acetylcholinesterase that promotes amyloid beta-peptide fibril formation.
Related PDB
Related UniProtKB
[51]
Resource
Comments
Medline ID
PubMed ID 11412096
Journal Biochemistry
Year 2001
Volume 40
Pages 7433-45
Authors Kaplan D, Ordentlich A, Barak D, Ariel N, Kronman C, Velan B, Shafferman A
Title Does "butyrylization" of acetylcholinesterase through substitution of the six divergent aromatic amino acids in the active center gorge generate an enzyme mimic of butyrylcholinesterase?
Related PDB
Related UniProtKB
[52]
Resource
Comments
Medline ID
PubMed ID 11341833
Journal Biochemistry
Year 2001
Volume 40
Pages 5682-90
Authors Massiah MA, Viragh C, Reddy PM, Kovach IM, Johnson J, Rosenberry TL, Mildvan AS
Title Short, strong hydrogen bonds at the active site of human acetylcholinesterase: proton NMR studies.
Related PDB
Related UniProtKB
[53]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11563919
Journal J Med Chem
Year 2001
Volume 44
Pages 3203-15
Authors Doucet-Personeni C, Bentley PD, Fletcher RJ, Kinkaid A, Kryger G, Pirard B, Taylor A, Taylor R, Taylor J, Viner R, Silman I, Sussman JL, Greenblatt HM, Lewis T
Title A structure-based design approach to the development of novel, reversible AChE inhibitors.
Related PDB 1hbj
Related UniProtKB
[54]
Resource
Comments
Medline ID
PubMed ID 11708910
Journal J Med Chem
Year 2001
Volume 44
Pages 4062-71
Authors Yu Q, Holloway HW, Flippen-Anderson JL, Hoffman B, Brossi A, Greig NH
Title Methyl analogues of the experimental Alzheimer drug phenserine: synthesis and structure/activity relationships for acetyl- and butyrylcholinesterase inhibitory action.
Related PDB
Related UniProtKB
[55]
Resource
Comments
Medline ID
PubMed ID 11449566
Journal J Mol Graph Model
Year 2001
Volume 19
Pages 288-96, 374-8
Authors Pilger C, Bartolucci C, Lamba D, Tropsha A, Fels G
Title Accurate prediction of the bound conformation of galanthamine in the active site of Torpedo californica acetylcholinesterase using molecular docking.
Related PDB
Related UniProtKB
[56]
Resource
Comments
Medline ID
PubMed ID 11567086
Journal Protein Sci
Year 2001
Volume 10
Pages 1953-61
Authors Weik M, Ravelli RB, Silman I, Sussman JL, Gros P, Kroon J
Title Specific protein dynamics near the solvent glass transition assayed by radiation-induced structural changes.
Related PDB
Related UniProtKB
[57]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11119642
Journal Proteins
Year 2001
Volume 42
Pages 182-91
Authors Bartolucci C, Perola E, Pilger C, Fels G, Lamba D
Title Three-dimensional structure of a complex of galanthamine (Nivalin) with acetylcholinesterase from Torpedo californica: implications for the design of new anti-Alzheimer drugs.
Related PDB 1qti
Related UniProtKB
[58]
Resource
Comments
Medline ID
PubMed ID 12069617
Journal Acc Chem Res
Year 2002
Volume 35
Pages 332-40
Authors Shen T, Tai K, Henchman RH, McCammon JA
Title Molecular dynamics of acetylcholinesterase.
Related PDB
Related UniProtKB
[59]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12351819
Journal Acta Crystallogr D Biol Crystallogr
Year 2002
Volume 58
Pages 1765-71
Authors Felder CE, Harel M, Silman I, Sussman JL
Title Structure of a complex of the potent and specific inhibitor BW284C51 with Torpedo californica acetylcholinesterase.
Related PDB 1e3q
Related UniProtKB
[60]
Resource
Comments
Medline ID
PubMed ID 12081473
Journal Biochemistry
Year 2002
Volume 41
Pages 8245-52
Authors Barak D, Kaplan D, Ordentlich A, Ariel N, Velan B, Shafferman A
Title The aromatic "trapping" of the catalytic histidine is essential for efficient catalysis in acetylcholinesterase.
Related PDB
Related UniProtKB
[61]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11888271
Journal Biochemistry
Year 2002
Volume 41
Pages 3555-64
Authors Bar-On P, Millard CB, Harel M, Dvir H, Enz A, Sussman JL, Silman I
Title Kinetic and structural studies on the interaction of cholinesterases with the anti-Alzheimer drug rivastigmine.
Related PDB 1gqr 1gqs
Related UniProtKB
[62]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12196020
Journal Biochemistry
Year 2002
Volume 41
Pages 10810-8
Authors Dvir H, Jiang HL, Wong DM, Harel M, Chetrit M, He XC, Jin GY, Yu GL, Tang XC, Silman I, Bai DL, Sussman JL
Title X-ray structures of Torpedo californica acetylcholinesterase complexed with (+)-huperzine A and (-)-huperzine B: structural evidence for an active site rearrangement.
Related PDB 1gpk 1gpn
Related UniProtKB
[63]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11863435
Journal Biochemistry
Year 2002
Volume 41
Pages 2970-81
Authors Dvir H, Wong DM, Harel M, Barril X, Orozco M, Luque FJ, Munoz-Torrero D, Camps P, Rosenberry TL, Silman I, Sussman JL
Title 3D structure of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 A resolution: kinetic and molecular dynamic correlates.
Related PDB 1e66
Related UniProtKB
[64]
Resource
Comments
Medline ID
PubMed ID 11904227
Journal Biochim Biophys Acta
Year 2002
Volume 1594
Pages 313-24
Authors Masson P, Schopfer LM, Bartels CF, Froment MT, Ribes F, Nachon F, Lockridge O
Title Substrate activation in acetylcholinesterase induced by low pH or mutation in the pi-cation subsite.
Related PDB
Related UniProtKB
[65]
Resource
Comments
Medline ID
PubMed ID 11920879
Journal Electrophoresis
Year 2002
Volume 23
Pages 930-7
Authors Rochu D, Renault F, Masson P
Title Detection of unwanted protein-bound ligands by capillary zone electrophoresis: the case of hidden ligands that stabilize cholinesterase conformation.
Related PDB
Related UniProtKB
[66]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12095250
Journal J Mol Biol
Year 2002
Volume 320
Pages 721-5
Authors Koellner G, Steiner T, Millard CB, Silman I, Sussman JL
Title A neutral molecule in a cation-binding site: specific binding of a PEG-SH to acetylcholinesterase from Torpedo californica.
Related PDB 1jjb
Related UniProtKB
[67]
Resource
Comments
Medline ID
PubMed ID 12731886
Journal Biochemistry
Year 2003
Volume 42
Pages 5438-52
Authors Johnson JL, Cusack B, Davies MP, Fauq A, Rosenberry TL
Title Unmasking tandem site interaction in human acetylcholinesterase. Substrate activation with a cationic acetanilide substrate.
Related PDB
Related UniProtKB
[68]
Resource
Comments
Medline ID
PubMed ID 12601798
Journal Biopolymers
Year 2003
Volume 68
Pages 395-406
Authors Zeev-Ben-Mordehai T, Silman I, Sussman JL
Title Acetylcholinesterase in motion: visualizing conformational changes in crystal structures by a morphing procedure.
Related PDB
Related UniProtKB
[69]
Resource
Comments
Medline ID
PubMed ID 12505979
Journal EMBO J
Year 2003
Volume 22
Pages 1-12
Authors Bourne Y, Taylor P, Radic Z, Marchot P
Title Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site.
Related PDB
Related UniProtKB
[70]
Resource
Comments
Medline ID
PubMed ID 14622273
Journal Eur J Biochem
Year 2003
Volume 270
Pages 4447-58
Authors Saxena A, Fedorko JM, Vinayaka CR, Medhekar R, Radic Z, Taylor P, Lockridge O, Doctor BP
Title Aromatic amino-acid residues at the active and peripheral anionic sites control the binding of E2020 (Aricept) to cholinesterases.
Related PDB
Related UniProtKB
[71]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID
Journal J Am Chem Soc
Year 2003
Volume 125
Pages 363-3
Authors Wong DM, Greenblatt HM, Dvir H, Carlier PR, Han YF, Pang YP, Silman I, Sussman JL
Title Acetylcholinesterase complexed with bivalent ligands related to huperzine A: experimental evidence for species-dependent protein-ligand complementarity.
Related PDB 1h22 1h23
Related UniProtKB
[72]
Resource
Comments
Medline ID
PubMed ID 12759360
Journal J Biol Chem
Year 2003
Volume 278
Pages 30905-11
Authors Shi J, Tai K, McCammon JA, Taylor P, Johnson DA
Title Nanosecond dynamics of the mouse acetylcholinesterase cys69-cys96 omega loop.
Related PDB
Related UniProtKB
[73]
Resource
Comments
Medline ID
PubMed ID 14584959
Journal J Med Chem
Year 2003
Volume 46
Pages 5087-90
Authors Zaheer-Ul-Haq ZU, Wellenzohn B, Liedl KR, Rode BM
Title Molecular docking studies of natural cholinesterase-inhibiting steroidal alkaloids from Sarcococca saligna.
Related PDB
Related UniProtKB
[74]
Resource
Comments
Medline ID
PubMed ID 15023064
Journal Biochemistry
Year 2004
Volume 43
Pages 3129-36
Authors Kaplan D, Barak D, Ordentlich A, Kronman C, Velan B, Shafferman A
Title Is aromaticity essential for trapping the catalytic histidine 447 in human acetylcholinesterase?
Related PDB
Related UniProtKB
[75]
Resource
Comments
Medline ID
PubMed ID 15078872
Journal J Biol Chem
Year 2004
Volume 279
Pages 26612-8
Authors Boyd AE, Dunlop CS, Wong L, Radic Z, Taylor P, Johnson DA
Title Nanosecond dynamics of acetylcholinesterase near the active center gorge.
Related PDB
Related UniProtKB
[76]
Resource
Comments
Medline ID
PubMed ID 15267237
Journal J Med Chem
Year 2004
Volume 47
Pages 3991-9
Authors Cavalli A, Bottegoni G, Raco C, De Vivo M, Recanatini M
Title A computational study of the binding of propidium to the peripheral anionic site of human acetylcholinesterase.
Related PDB
Related UniProtKB
[77]
Resource
Comments
Medline ID
PubMed ID 15563167
Journal J Am Chem Soc
Year 2004
Volume 126
Pages 15405-11
Authors Greenblatt HM, Guillou C, Guenard D, Argaman A, Botti S, Badet B, Thal C, Silman I, Sussman JL
Title 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.
Related PDB 1w4l 1w6r 1w75 1w76
Related UniProtKB

Comments
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.)

Created Updated
2004-03-19 2012-02-21