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Acetylcholinesterase (AChE) (EC 3.1.1.7)

 ACES_TETCF              Reviewed;         586 AA.
P04058;
01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 2.
25-OCT-2017, entry version 155.
RecName: Full=Acetylcholinesterase;
Short=AChE;
EC=3.1.1.7;
Flags: Precursor;
Name=ache;
Tetronarce californica (Pacific electric ray) (Torpedo californica).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Tetronarce.
NCBI_TaxID=7787;
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 10-586.
PubMed=3753747; DOI=10.1038/319407a0;
Schumacher M., Camp S., Maulet Y., Newton M., McPhee-Quigley K.,
Taylor S.S., Friedmann T., Taylor P.;
"Primary structure of Torpedo californica acetylcholinesterase deduced
from its cDNA sequence.";
Nature 319:407-409(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
PubMed=3198606;
Schumacher M.;
"Multiple messenger RNA species give rise to the structural diversity
in acetylcholinesterase.";
J. Biol. Chem. 263:18979-18987(1988).
[3]
PROTEIN SEQUENCE OF 22-45 AND 214-237.
PubMed=3900071;
MacPhee-Quigley K., Taylor P., Taylor S.;
"Primary structures of the catalytic subunits from two molecular forms
of acetylcholinesterase. A comparison of NH2-terminal and active
center sequences.";
J. Biol. Chem. 260:12185-12189(1985).
[4]
PROTEIN SEQUENCE OF 100-108.
PubMed=2068091; DOI=10.1073/pnas.88.14.6117;
Kreienkamp H.J., Weise C., Raba R., Aaviksaar A., Hucho F.;
"Anionic subsites of the catalytic center of acetylcholinesterase from
Torpedo and from cobra venom.";
Proc. Natl. Acad. Sci. U.S.A. 88:6117-6121(1991).
[5]
PROTEIN SEQUENCE OF 552-558.
PubMed=3335534;
Gibney G., Macphee-Quigley K., Thompson B., Vedvick T., Low M.G.,
Taylor S.S., Taylor P.;
"Divergence in primary structure between the molecular forms of
acetylcholinesterase.";
J. Biol. Chem. 263:1140-1145(1988).
[6]
ALTERNATIVE SPLICING.
PubMed=2306366; DOI=10.1016/0896-6273(90)90103-M;
Maulet Y., Camp S., Gibney G., Rachinsky T.L., Ekstroem T.J.,
Taylor P.;
"Single gene encodes glycophospholipid-anchored and asymmetric
acetylcholinesterase forms: alternative coding exons contain inverted
repeat sequences.";
Neuron 4:289-301(1990).
[7]
DISULFIDE BONDS.
PubMed=3759980;
McPhee-Quigley K., Vedvick T.S., Taylor P., Taylor S.S.;
"Profile of the disulfide bonds in acetylcholinesterase.";
J. Biol. Chem. 261:13565-13570(1986).
[8]
STRUCTURE OF THE GPI-ANCHOR.
PubMed=8257440; DOI=10.1042/bj2960473;
Mehlert A., Varon L., Silman I., Homans S.W., Ferguson M.A.;
"Structure of the glycosyl-phosphatidylinositol membrane anchor of
acetylcholinesterase from the electric organ of the electric-fish,
Torpedo californica.";
Biochem. J. 296:473-479(1993).
[9]
GPI-ANCHOR AT SER-564.
PubMed=8597567; DOI=10.1016/0167-4838(95)00205-7;
Bucht G., Hjalmarsson K.;
"Residues in Torpedo californica acetylcholinesterase necessary for
processing to a glycosyl phosphatidylinositol-anchored form.";
Biochim. Biophys. Acta 1292:223-232(1996).
[10]
MUTAGENESIS.
PubMed=2217185; DOI=10.1073/pnas.87.19.7546;
Gibney G., Camp S., Dionne M., McPhee-Quigley K., Taylor P.;
"Mutagenesis of essential functional residues in
acetylcholinesterase.";
Proc. Natl. Acad. Sci. U.S.A. 87:7546-7550(1990).
[11]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-558, ACTIVE SITE,
GLYCOSYLATION AT ASN-437, DISULFIDE BONDS, AND SUBUNIT.
PubMed=1678899; DOI=10.1126/science.1678899;
Sussman J.L., Harel M., Frolow F., Oefner C., Goldman A., Toker L.,
Silman I.;
"Atomic structure of acetylcholinesterase from Torpedo californica: a
prototypic acetylcholine-binding protein.";
Science 253:872-879(1991).
[12]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-556 IN COMPLEX WITH
SUBSTRATE ANALOGS.
PubMed=8415649; DOI=10.1073/pnas.90.19.9031;
Harel M., Schalk I., Ehret-Sabatier L., Bouet F., Goeldner M.,
Hirth C., Axelsen P.H., Silman I., Sussman J.L.;
"Quaternary ligand binding to aromatic residues in the active-site
gorge of acetylcholinesterase.";
Proc. Natl. Acad. Sci. U.S.A. 90:9031-9035(1993).
[13]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 22-558 IN COMPLEX WITH
FASCICULIN-2, AND DISULFIDE BOND.
PubMed=8747462; DOI=10.1016/S0969-2126(01)00273-8;
Harel M., Kleywegt G.J., Ravelli R.B., Silman I., Sussman J.L.;
"Crystal structure of an acetylcholinesterase-fasciculin complex:
interaction of a three-fingered toxin from snake venom with its
target.";
Structure 3:1355-1366(1995).
[14]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-558 IN COMPLEX WITH THE
INHIBITOR HUPERZINE A.
PubMed=8989325; DOI=10.1038/nsb0197-57;
Raves M.L., Harel M., Pang Y.P., Silman I., Kozikowski A.P.,
Sussman J.L.;
"Structure of acetylcholinesterase complexed with the nootropic
alkaloid, (-)-huperzine A.";
Nat. Struct. Biol. 4:57-63(1997).
[15]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-558.
PubMed=10231521; DOI=10.1021/bi982723p;
Bartolucci C., Perola E., Cellai L., Brufani M., Lamba D.;
"'Back door' opening implied by the crystal structure of a
carbamoylated acetylcholinesterase.";
Biochemistry 38:5714-5719(1999).
[16]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-558.
PubMed=10353814; DOI=10.1021/bi982678l;
Millard C.B., Kryger G., Ordentlich A., Greenblatt H.M., Harel M.,
Raves M.L., Segall Y., Barak D., Shafferman A., Silman I.,
Sussman J.L.;
"Crystal structures of aged phosphonylated acetylcholinesterase: nerve
agent reaction products at the atomic level.";
Biochemistry 38:7032-7039(1999).
[17]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-564 IN COMPLEX WITH
GALANTHAMINE.
PubMed=10606746; DOI=10.1016/S0014-5793(99)01637-3;
Greenblatt H.M., Kryger G., Lewis T., Silman I., Sussman J.L.;
"Structure of acetylcholinesterase complexed with (-)-galanthamine at
2.3-A resolution.";
FEBS Lett. 463:321-326(1999).
[18]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-564 IN COMPLEX WITH THE
SYNTHETIC INHIBITOR ARICEPT, AND GLYCOSYLATION AT ASN-80; ASN-437;
ASN-478 AND ASN-554.
PubMed=10368299; DOI=10.1016/S0969-2126(99)80040-9;
Kryger G., Silman I., Sussman J.L.;
"Structure of acetylcholinesterase complexed with E2020 (Aricept(R)):
implications for the design of new anti-Alzheimer drugs.";
Structure 7:297-307(1999).
[19]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 22-564 IN COMPLEX WITH THE
SYNTHETIC INHIBITOR HUPRINE.
PubMed=11863435; DOI=10.1021/bi011652i;
Dvir H., Wong D.M., Harel M., Barril X., Orozco M., Luque F.J.,
Munoz-Torrero D., Camps P., Rosenberry T.L., Silman I., Sussman J.L.;
"3D structure of Torpedo californica acetylcholinesterase complexed
with huprine X at 2.1 A resolution: kinetic and molecular dynamic
correlates.";
Biochemistry 41:2970-2981(2002).
[20]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-556 IN COMPLEX WITH THE
SYNTHETIC INHIBITOR RIVASTIGMINE.
PubMed=11888271; DOI=10.1021/bi020016x;
Bar-On P., Millard C.B., Harel M., Dvir H., Enz A., Sussman J.L.,
Silman I.;
"Kinetic and structural studies on the interaction of cholinesterases
with the anti-Alzheimer drug rivastigmine.";
Biochemistry 41:3555-3564(2002).
[21]
X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 22-564 IN COMPLEX WITH THE
SYNTHETIC INHIBITOR CPT-11.
PubMed=15772291; DOI=10.1124/mol.104.009944;
Harel M., Hyatt J.L., Brumshtein B., Morton C.L., Yoon K.J.,
Wadkins R.M., Silman I., Sussman J.L., Potter P.M.;
"The crystal structure of the complex of the anticancer prodrug 7-
ethyl-10-[4-(1-piperidino)-1-piperidino]-carbonyloxycamptothecin (CPT-
11) with Torpedo californica acetylcholinesterase provides a molecular
explanation for its cholinergic action.";
Mol. Pharmacol. 67:1874-1881(2005).
[22]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 22-558 IN COMPLEXES WITH
SUBSTRATE AND SUBSTRATE ANALOGS, GLYCOSYLATION AT ASN-80 AND ASN-437,
ACTIVE SITE, AND ENZYME REGULATION.
PubMed=16763558; DOI=10.1038/sj.emboj.7601175;
Colletier J.-P., Fournier D., Greenblatt H.M., Stojan J.,
Sussman J.L., Zaccai G., Silman I., Weik M.;
"Structural insights into substrate traffic and inhibition in
acetylcholinesterase.";
EMBO J. 25:2746-2756(2006).
[23]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 22-558 IN COMPLEX WITH SOMAN,
ACTIVE SITE, AND DISULFIDE BONDS.
PubMed=19642642; DOI=10.1021/jm900433t;
Sanson B., Nachon F., Colletier J.P., Froment M.T., Toker L.,
Greenblatt H.M., Sussman J.L., Ashani Y., Masson P., Silman I.,
Weik M.;
"Crystallographic snapshots of nonaged and aged conjugates of soman
with acetylcholinesterase, and of a ternary complex of the aged
conjugate with pralidoxime.";
J. Med. Chem. 52:7593-7603(2009).
[24]
X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 23-556 IN COMPLEX WITH
GALANTHAMINE DERIVATIVES.
PubMed=20025280; DOI=10.1021/jm901296p;
Bartolucci C., Haller L.A., Jordis U., Fels G., Lamba D.;
"Probing Torpedo californica acetylcholinesterase catalytic gorge with
two novel bis-functional galanthamine derivatives.";
J. Med. Chem. 53:745-751(2010).
-!- FUNCTION: Terminates signal transduction at the neuromuscular
junction by rapid hydrolysis of the acetylcholine released into
the synaptic cleft. May be involved in cell-cell interactions.
-!- CATALYTIC ACTIVITY: Acetylcholine + H(2)O = choline + acetate.
-!- ENZYME REGULATION: Inhibited by substrate concentrations above 0.5
mM. {ECO:0000269|PubMed:16763558}.
-!- SUBUNIT: Isoform H form is a homodimer; the asymmetric form is a
disulfide-bonded oligomer composed of a collagenic subunit (Q) and
a variable number of T catalytic subunits.
{ECO:0000269|PubMed:10368299, ECO:0000269|PubMed:10606746,
ECO:0000269|PubMed:11863435, ECO:0000269|PubMed:11888271,
ECO:0000269|PubMed:15772291, ECO:0000269|PubMed:1678899,
ECO:0000269|PubMed:19642642, ECO:0000269|PubMed:20025280,
ECO:0000269|PubMed:8415649, ECO:0000269|PubMed:8747462,
ECO:0000269|PubMed:8989325}.
-!- SUBCELLULAR LOCATION: Isoform H: Cell membrane; Lipid-anchor, GPI-
anchor. Cell junction, synapse.
-!- SUBCELLULAR LOCATION: 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist.;
Name=H; Synonyms=Globular;
IsoId=P04058-1; Sequence=Displayed;
Note=GPI-anchored form.;
Name=T;
IsoId=P04058-2; Sequence=VSP_001460;
-!- TISSUE SPECIFICITY: Found in the synapses and to a lower extent in
extrajunctional areas of muscle and nerve, and on erythrocyte
membranes.
-!- PTM: An interchain disulfide bond is present in what becomes
position 593 of the T isoform.
-!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
{ECO:0000305}.
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EMBL; X03439; CAA27169.1; -; mRNA.
EMBL; X56516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X56517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A00773; ACRYE.
PDB; 1ACJ; X-ray; 2.80 A; A=22-556.
PDB; 1ACL; X-ray; 2.80 A; A=22-556.
PDB; 1AMN; X-ray; 2.80 A; A=22-558.
PDB; 1AX9; X-ray; 2.80 A; A=22-558.
PDB; 1CFJ; X-ray; 2.60 A; A=22-558.
PDB; 1DX6; X-ray; 2.30 A; A=22-564.
PDB; 1E3Q; X-ray; 2.85 A; A=22-564.
PDB; 1E66; X-ray; 2.10 A; A=22-564.
PDB; 1EA5; X-ray; 1.80 A; A=22-558.
PDB; 1EEA; X-ray; 4.50 A; A=22-555.
PDB; 1EVE; X-ray; 2.50 A; A=22-564.
PDB; 1FSS; X-ray; 3.00 A; A=22-558.
PDB; 1GPK; X-ray; 2.10 A; A=22-558.
PDB; 1GPN; X-ray; 2.35 A; A=22-558.
PDB; 1GQR; X-ray; 2.20 A; A=25-556.
PDB; 1GQS; X-ray; 3.00 A; A=25-556.
PDB; 1H22; X-ray; 2.15 A; A=22-564.
PDB; 1H23; X-ray; 2.15 A; A=22-564.
PDB; 1HBJ; X-ray; 2.50 A; A=22-564.
PDB; 1JGA; Model; -; A=1-586.
PDB; 1JGB; Model; -; A=1-586.
PDB; 1JJB; X-ray; 2.30 A; A=25-556.
PDB; 1OCE; X-ray; 2.70 A; A=22-558.
PDB; 1ODC; X-ray; 2.20 A; A=22-564.
PDB; 1QID; X-ray; 2.05 A; A=22-558.
PDB; 1QIE; X-ray; 2.10 A; A=22-558.
PDB; 1QIF; X-ray; 2.10 A; A=22-558.
PDB; 1QIG; X-ray; 2.30 A; A=22-558.
PDB; 1QIH; X-ray; 2.50 A; A=22-558.
PDB; 1QII; X-ray; 2.65 A; A=22-558.
PDB; 1QIJ; X-ray; 2.80 A; A=22-558.
PDB; 1QIK; X-ray; 2.90 A; A=22-558.
PDB; 1QIM; X-ray; 3.00 A; A=22-558.
PDB; 1QTI; X-ray; 2.50 A; A=22-558.
PDB; 1SOM; X-ray; 2.20 A; A=22-564.
PDB; 1U65; X-ray; 2.61 A; A=22-564.
PDB; 1UT6; X-ray; 2.40 A; A=22-556.
PDB; 1VOT; X-ray; 2.50 A; A=22-558.
PDB; 1VXO; X-ray; 2.40 A; A=22-558.
PDB; 1VXR; X-ray; 2.20 A; A=22-558.
PDB; 1W4L; X-ray; 2.16 A; A=22-564.
PDB; 1W6R; X-ray; 2.05 A; A=22-564.
PDB; 1W75; X-ray; 2.40 A; A/B=22-564.
PDB; 1W76; X-ray; 2.30 A; A/B=22-564.
PDB; 1ZGB; X-ray; 2.30 A; A=22-564.
PDB; 1ZGC; X-ray; 2.10 A; A/B=22-564.
PDB; 2ACE; X-ray; 2.50 A; A=22-558.
PDB; 2ACK; X-ray; 2.40 A; A=22-558.
PDB; 2BAG; X-ray; 2.40 A; A=22-564.
PDB; 2C4H; X-ray; 2.15 A; A=22-558.
PDB; 2C58; X-ray; 2.30 A; A=22-558.
PDB; 2C5F; X-ray; 2.60 A; A=22-558.
PDB; 2C5G; X-ray; 1.95 A; A=22-558.
PDB; 2CEK; X-ray; 2.20 A; A=22-556.
PDB; 2CKM; X-ray; 2.15 A; A=22-564.
PDB; 2CMF; X-ray; 2.50 A; A=22-564.
PDB; 2DFP; X-ray; 2.30 A; A=23-556.
PDB; 2J3D; X-ray; 2.60 A; A=22-564.
PDB; 2J3Q; X-ray; 2.80 A; A=22-564.
PDB; 2J4F; X-ray; 2.80 A; A=22-564.
PDB; 2V96; X-ray; 2.40 A; A/B=22-558.
PDB; 2V97; X-ray; 2.40 A; A/B=22-558.
PDB; 2V98; X-ray; 3.00 A; A/B=22-558.
PDB; 2VA9; X-ray; 2.40 A; A/B=22-558.
PDB; 2VJA; X-ray; 2.30 A; A/B=22-558.
PDB; 2VJB; X-ray; 2.39 A; A/B=22-558.
PDB; 2VJC; X-ray; 2.20 A; A/B=22-558.
PDB; 2VJD; X-ray; 2.30 A; A/B=22-558.
PDB; 2VQ6; X-ray; 2.71 A; A=22-564.
PDB; 2VT6; X-ray; 2.40 A; A/B=22-558.
PDB; 2VT7; X-ray; 2.20 A; A/B=22-558.
PDB; 2W6C; X-ray; 2.69 A; X=1-586.
PDB; 2WFZ; X-ray; 1.95 A; A=22-558.
PDB; 2WG0; X-ray; 2.20 A; A=22-558.
PDB; 2WG1; X-ray; 2.20 A; A=22-558.
PDB; 2WG2; X-ray; 1.95 A; A=22-558.
PDB; 2XI4; X-ray; 2.30 A; A/B=22-558.
PDB; 3ACE; Model; -; A=22-558.
PDB; 3GEL; X-ray; 2.39 A; A=25-556.
PDB; 3I6M; X-ray; 2.26 A; A=23-556.
PDB; 3I6Z; X-ray; 2.19 A; A=23-556.
PDB; 3M3D; X-ray; 2.34 A; A=22-564.
PDB; 3ZV7; X-ray; 2.26 A; A=22-564.
PDB; 4ACE; Model; -; A=22-558.
PDB; 4TVK; X-ray; 2.30 A; A=23-556.
PDB; 4W63; X-ray; 2.80 A; A=23-556.
PDB; 4X3C; X-ray; 2.60 A; A=23-556.
PDB; 5BWB; X-ray; 2.57 A; A=22-558.
PDB; 5BWC; X-ray; 2.45 A; A=22-558.
PDB; 5DLP; X-ray; 2.70 A; A=22-564.
PDB; 5E2I; X-ray; 2.65 A; A=25-556.
PDB; 5E4J; X-ray; 2.54 A; A=25-556.
PDB; 5E4T; X-ray; 2.43 A; A=22-564.
PDB; 5EHX; X-ray; 2.10 A; A=25-556.
PDB; 5EI5; X-ray; 2.10 A; A=23-556.
PDB; 5IH7; X-ray; 2.40 A; A=23-556.
PDBsum; 1ACJ; -.
PDBsum; 1ACL; -.
PDBsum; 1AMN; -.
PDBsum; 1AX9; -.
PDBsum; 1CFJ; -.
PDBsum; 1DX6; -.
PDBsum; 1E3Q; -.
PDBsum; 1E66; -.
PDBsum; 1EA5; -.
PDBsum; 1EEA; -.
PDBsum; 1EVE; -.
PDBsum; 1FSS; -.
PDBsum; 1GPK; -.
PDBsum; 1GPN; -.
PDBsum; 1GQR; -.
PDBsum; 1GQS; -.
PDBsum; 1H22; -.
PDBsum; 1H23; -.
PDBsum; 1HBJ; -.
PDBsum; 1JGA; -.
PDBsum; 1JGB; -.
PDBsum; 1JJB; -.
PDBsum; 1OCE; -.
PDBsum; 1ODC; -.
PDBsum; 1QID; -.
PDBsum; 1QIE; -.
PDBsum; 1QIF; -.
PDBsum; 1QIG; -.
PDBsum; 1QIH; -.
PDBsum; 1QII; -.
PDBsum; 1QIJ; -.
PDBsum; 1QIK; -.
PDBsum; 1QIM; -.
PDBsum; 1QTI; -.
PDBsum; 1SOM; -.
PDBsum; 1U65; -.
PDBsum; 1UT6; -.
PDBsum; 1VOT; -.
PDBsum; 1VXO; -.
PDBsum; 1VXR; -.
PDBsum; 1W4L; -.
PDBsum; 1W6R; -.
PDBsum; 1W75; -.
PDBsum; 1W76; -.
PDBsum; 1ZGB; -.
PDBsum; 1ZGC; -.
PDBsum; 2ACE; -.
PDBsum; 2ACK; -.
PDBsum; 2BAG; -.
PDBsum; 2C4H; -.
PDBsum; 2C58; -.
PDBsum; 2C5F; -.
PDBsum; 2C5G; -.
PDBsum; 2CEK; -.
PDBsum; 2CKM; -.
PDBsum; 2CMF; -.
PDBsum; 2DFP; -.
PDBsum; 2J3D; -.
PDBsum; 2J3Q; -.
PDBsum; 2J4F; -.
PDBsum; 2V96; -.
PDBsum; 2V97; -.
PDBsum; 2V98; -.
PDBsum; 2VA9; -.
PDBsum; 2VJA; -.
PDBsum; 2VJB; -.
PDBsum; 2VJC; -.
PDBsum; 2VJD; -.
PDBsum; 2VQ6; -.
PDBsum; 2VT6; -.
PDBsum; 2VT7; -.
PDBsum; 2W6C; -.
PDBsum; 2WFZ; -.
PDBsum; 2WG0; -.
PDBsum; 2WG1; -.
PDBsum; 2WG2; -.
PDBsum; 2XI4; -.
PDBsum; 3ACE; -.
PDBsum; 3GEL; -.
PDBsum; 3I6M; -.
PDBsum; 3I6Z; -.
PDBsum; 3M3D; -.
PDBsum; 3ZV7; -.
PDBsum; 4ACE; -.
PDBsum; 4TVK; -.
PDBsum; 4W63; -.
PDBsum; 4X3C; -.
PDBsum; 5BWB; -.
PDBsum; 5BWC; -.
PDBsum; 5DLP; -.
PDBsum; 5E2I; -.
PDBsum; 5E4J; -.
PDBsum; 5E4T; -.
PDBsum; 5EHX; -.
PDBsum; 5EI5; -.
PDBsum; 5IH7; -.
ProteinModelPortal; P04058; -.
SMR; P04058; -.
MINT; MINT-1518870; -.
BindingDB; P04058; -.
ChEMBL; CHEMBL4780; -.
ESTHER; torca-ACHE; AChE.
MEROPS; S09.980; -.
iPTMnet; P04058; -.
HOVERGEN; HBG008839; -.
BioCyc; MetaCyc:MONOMER-16823; -.
BRENDA; 3.1.1.7; 6395.
EvolutionaryTrace; P04058; -.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0043083; C:synaptic cleft; IEA:GOC.
GO; GO:0003990; F:acetylcholinesterase activity; IEA:UniProtKB-EC.
GO; GO:0001507; P:acetylcholine catabolic process in synaptic cleft; IEA:InterPro.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR000908; Acylcholinesterase_fish/snake.
InterPro; IPR002018; CarbesteraseB.
InterPro; IPR019826; Carboxylesterase_B_AS.
InterPro; IPR019819; Carboxylesterase_B_CS.
InterPro; IPR000997; Cholinesterase.
Pfam; PF00135; COesterase; 1.
PRINTS; PR00879; ACHEFISH.
PRINTS; PR00878; CHOLNESTRASE.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
Hydrolase; Lipoprotein; Membrane; Neurotransmitter degradation;
Serine esterase; Signal; Synapse.
SIGNAL 1 21 {ECO:0000269|PubMed:3900071}.
CHAIN 22 564 Acetylcholinesterase.
/FTId=PRO_0000008595.
PROPEP 565 586 Removed in mature form.
/FTId=PRO_0000008596.
ACT_SITE 221 221 Acyl-ester intermediate.
ACT_SITE 348 348 Charge relay system.
ACT_SITE 461 461 Charge relay system.
LIPID 564 564 GPI-anchor amidated serine.
{ECO:0000269|PubMed:8597567}.
CARBOHYD 80 80 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10368299,
ECO:0000269|PubMed:16763558}.
CARBOHYD 437 437 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10368299,
ECO:0000269|PubMed:16763558,
ECO:0000269|PubMed:1678899}.
CARBOHYD 478 478 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10368299}.
CARBOHYD 554 554 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10368299}.
DISULFID 88 115
DISULFID 275 286
DISULFID 423 542
DISULFID 558 558 Interchain.
VAR_SEQ 557 586 ACDGELSSSGTSSSKGIIFYVLFSILYLIF -> ETIDEAE
RQWKTEFHRWSSYMMHWKNQFDHYSRHESCAEL (in
isoform T). {ECO:0000305}.
/FTId=VSP_001460.
MUTAGEN 220 220 E->H: Loss of activity.
{ECO:0000269|PubMed:2217185}.
MUTAGEN 220 220 E->Q,D: Decrease in activity.
{ECO:0000269|PubMed:2217185}.
MUTAGEN 221 221 S->C: Loss of activity.
{ECO:0000269|PubMed:2217185}.
MUTAGEN 221 221 S->V: Loss of activity.
{ECO:0000269|PubMed:2217185}.
MUTAGEN 446 446 H->Q: Almost no loss of activity.
{ECO:0000269|PubMed:2217185}.
MUTAGEN 461 461 H->Q: Loss of activity.
{ECO:0000269|PubMed:2217185}.
STRAND 28 31 {ECO:0000244|PDB:1EA5}.
STRAND 34 37 {ECO:0000244|PDB:1EA5}.
STRAND 39 43 {ECO:0000244|PDB:1EA5}.
STRAND 46 55 {ECO:0000244|PDB:1EA5}.
HELIX 62 64 {ECO:0000244|PDB:1EA5}.
STRAND 76 80 {ECO:0000244|PDB:1EA5}.
STRAND 87 89 {ECO:0000244|PDB:2CMF}.
STRAND 95 98 {ECO:0000244|PDB:1OCE}.
HELIX 100 103 {ECO:0000244|PDB:1EA5}.
STRAND 111 113 {ECO:0000244|PDB:3ZV7}.
STRAND 117 122 {ECO:0000244|PDB:1EA5}.
STRAND 128 136 {ECO:0000244|PDB:1EA5}.
TURN 140 142 {ECO:0000244|PDB:1EA5}.
HELIX 149 151 {ECO:0000244|PDB:1EA5}.
HELIX 154 160 {ECO:0000244|PDB:1EA5}.
STRAND 163 166 {ECO:0000244|PDB:1EA5}.
HELIX 172 176 {ECO:0000244|PDB:1EA5}.
STRAND 183 185 {ECO:0000244|PDB:1EA5}.
HELIX 189 204 {ECO:0000244|PDB:1EA5}.
HELIX 205 208 {ECO:0000244|PDB:1EA5}.
STRAND 210 220 {ECO:0000244|PDB:1EA5}.
HELIX 222 232 {ECO:0000244|PDB:1EA5}.
HELIX 234 237 {ECO:0000244|PDB:1EA5}.
STRAND 241 247 {ECO:0000244|PDB:1EA5}.
TURN 253 255 {ECO:0000244|PDB:1QID}.
HELIX 259 272 {ECO:0000244|PDB:1EA5}.
HELIX 280 289 {ECO:0000244|PDB:1EA5}.
HELIX 292 298 {ECO:0000244|PDB:1EA5}.
HELIX 299 302 {ECO:0000244|PDB:1EA5}.
STRAND 304 306 {ECO:0000244|PDB:1EA5}.
STRAND 307 309 {ECO:0000244|PDB:4W63}.
STRAND 319 324 {ECO:0000244|PDB:1EA5}.
HELIX 326 332 {ECO:0000244|PDB:1EA5}.
STRAND 340 345 {ECO:0000244|PDB:1EA5}.
STRAND 347 349 {ECO:0000244|PDB:2WFZ}.
HELIX 350 356 {ECO:0000244|PDB:1EA5}.
STRAND 362 364 {ECO:0000244|PDB:2WG1}.
HELIX 370 380 {ECO:0000244|PDB:1EA5}.
HELIX 386 395 {ECO:0000244|PDB:1EA5}.
TURN 399 401 {ECO:0000244|PDB:2CMF}.
HELIX 405 420 {ECO:0000244|PDB:1EA5}.
HELIX 422 433 {ECO:0000244|PDB:1EA5}.
STRAND 435 437 {ECO:0000244|PDB:2J3Q}.
STRAND 439 444 {ECO:0000244|PDB:1EA5}.
HELIX 455 457 {ECO:0000244|PDB:1EA5}.
TURN 461 464 {ECO:0000244|PDB:1EA5}.
HELIX 465 468 {ECO:0000244|PDB:1EA5}.
HELIX 471 473 {ECO:0000244|PDB:1EA5}.
HELIX 475 477 {ECO:0000244|PDB:1EA5}.
HELIX 481 500 {ECO:0000244|PDB:1EA5}.
STRAND 501 504 {ECO:0000244|PDB:2CKM}.
TURN 518 520 {ECO:0000244|PDB:1EA5}.
STRAND 522 529 {ECO:0000244|PDB:1EA5}.
STRAND 533 536 {ECO:0000244|PDB:1EA5}.
HELIX 539 546 {ECO:0000244|PDB:1EA5}.
HELIX 548 555 {ECO:0000244|PDB:1EA5}.
SEQUENCE 586 AA; 65906 MW; 731D5F0F3ABA62A8 CRC64;
MNLLVTSSLG VLLHLVVLCQ ADDHSELLVN TKSGKVMGTR VPVLSSHISA FLGIPFAEPP
VGNMRFRRPE PKKPWSGVWN ASTYPNNCQQ YVDEQFPGFS GSEMWNPNRE MSEDCLYLNI
WVPSPRPKST TVMVWIYGGG FYSGSSTLDV YNGKYLAYTE EVVLVSLSYR VGAFGFLALH
GSQEAPGNVG LLDQRMALQW VHDNIQFFGG DPKTVTIFGE SAGGASVGMH ILSPGSRDLF
RRAILQSGSP NCPWASVSVA EGRRRAVELG RNLNCNLNSD EELIHCLREK KPQELIDVEW
NVLPFDSIFR FSFVPVIDGE FFPTSLESML NSGNFKKTQI LLGVNKDEGS FFLLYGAPGF
SKDSESKISR EDFMSGVKLS VPHANDLGLD AVTLQYTDWM DDNNGIKNRD GLDDIVGDHN
VICPLMHFVN KYTKFGNGTY LYFFNHRASN LVWPEWMGVI HGYEIEFVFG LPLVKELNYT
AEEEALSRRI MHYWATFAKT GNPNEPHSQE SKWPLFTTKE QKFIDLNTEP MKVHQRLRVQ
MCVFWNQFLP KLLNATACDG ELSSSGTSSS KGIIFYVLFS ILYLIF


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