Cloned (Comment) | Organism |
---|---|
gene ace1, sequence comparisons and phylogenetic analysis | Tetranychus urticae |
gene ace1, sequence comparisons and phylogenetic analysis, recombinant expression of isozyme PpAChE1 in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system | Pardosa pseudoannulata |
gene ace2, sequence comparisons and phylogenetic analysis, recombinant expression of isozyme PpAChE2 in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system | Pardosa pseudoannulata |
gene ace3, sequence comparisons and phylogenetic analysis, recombinant expression of isozyme PpAChE3 in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system | Pardosa pseudoannulata |
gene ace4, sequence comparisons and phylogenetic analysis, recombinant expression of isozyme PpAChE4 in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system | Pardosa pseudoannulata |
gene ace5, sequence comparisons and phylogenetic analysis, recombinant expression of isozyme PpAChE5 as EGFP-tagged protein in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system | Pardosa pseudoannulata |
gene ache, sequence comparisons and phylogenetic analysis | Tetronarce californica |
Crystallization (Comment) | Organism |
---|---|
analysis of crystal structure PDB ID 4ey4 | Tetronarce californica |
analysis of crystal structure PDB ID 4ey4 | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
(7R,11R)-huprine 19 | huprines are a family of nano- to femtomolar inhibitors of AChE with specificity for the A-site interaction. The main feature is the remarkable embedding of the chloroquinolinium moiety into an aromatic stacking pile involving Trp86/HuprineW/Tyr337/Phe338/Phe295/Trp236 | Homo sapiens | |
(7R,11R)-huprine 19 | huprines are a family of nano- to femtomolar inhibitors of AChE with specificity for the A-site interaction. The main feature is the remarkable embedding of the chloroquinolinium moiety into an aromatic stacking pile involving Trp86/HuprineW/Tyr337/Phe338/Phe295/Trp236 | Tetronarce californica | |
(7S,11S)-huprine W | huprines are a family of nano- to femtomolar inhibitors of AChE with specificity for the A-site interaction. The main feature is the remarkable embedding of the chloroquinolinium moiety into an aromatic stacking pile involving Trp86/HuprineW/Tyr337/Phe338/Phe295/Trp236 | Homo sapiens | |
(7S,11S)-huprine W | huprines are a family of nano- to femtomolar inhibitors of AChE with specificity for the A-site interaction. The main feature is the remarkable embedding of the chloroquinolinium moiety into an aromatic stacking pile involving Trp86/HuprineW/Tyr337/Phe338/Phe295/Trp236 | Tetronarce californica | |
BW284c51 | 1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide; 1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide; 1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide; 1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide; 1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide | Pardosa pseudoannulata | |
Carbaryl | - |
Pardosa pseudoannulata | |
decamethonium | decamethonium is a prototypical dual binding site ligand of AChE that spans the active site gorge from the P-site to the choline binding pocket in the A-site | Homo sapiens | |
decamethonium | decamethonium is a prototypical dual binding site ligand of AChE that spans the active site gorge from the P-site to the choline binding pocket in the A-site, where it is stabilized by the cation-Pi interactions illustrated in its complex with Torpedo californica AChE (TcAChE), binding structure, overview | Tetronarce californica | |
diazoxon | - |
Pardosa pseudoannulata | |
edrophonium | - |
Homo sapiens | |
edrophonium | - |
Tetronarce californica | |
eserine | - |
Pardosa pseudoannulata | |
ethopropazine | ethopropazine is a substituted phenothiazine with a marked specificity for BChE. The 9000fold difference in Ki between hAChE and hBChE (EC 3.1.1.8) reflects this specificity | Homo sapiens | |
ethopropazine | - |
Tetronarce californica | |
fenobucarb | - |
Pardosa pseudoannulata | |
iso-ompa | tetraisopropyl diphosphoramide, inhibition of activity with butyrylthiocholine | Pardosa pseudoannulata | |
additional information | determination and analysis of the crystal structures of enzyme-bound ligands | Homo sapiens | |
additional information | no inhibition of activity with butyrylthiocholine by ISO-OMPA (tetraisopropyl diphosphoramide); no inhibition of activity with butyrylthiocholine by ISO-OMPA (tetraisopropyl diphosphoramide); no inhibition of activity with butyrylthiocholine by ISO-OMPA (tetraisopropyl diphosphoramide); no inhibition of activity with butyrylthiocholine by ISO-OMPA (tetraisopropyl diphosphoramide) | Pardosa pseudoannulata | |
additional information | determination and analysis of the crystal structures of enzyme-bound ligands | Tetronarce californica | |
paraoxon | - |
Pardosa pseudoannulata | |
propidium | - |
Homo sapiens | |
propidium | structure of the complex is solved at 3.0 A resolution, absence involving Trp279 in TcAChE at the gorge | Tetronarce californica | |
thioflavin T | - |
Homo sapiens | |
thioflavin T | ThT, is not sufficiently long to span the P-site and the choline binding site pocket of enzyme TcAChE. The benzothiazole and dimethylaminophenyl rings, and the dimethylamino group of this ligand are coplanar and lay parallel to Trp279 and Tyr334 and Phe330, respectively. The dimethylamino group is at 3.3 A from the aromatic ring of Phe330 but remains far from the gorge bottom, at a distance of 8.5 A from the carboxylate oxygens of Glu199. This position at the P-site allows concomitant binding of A-site ligands like edrophonium or m-(N,N,N-trimethylammonio)trifluoroacetophenone (TMTFA) through an adjustment of the orientation of Phe330 | Tetronarce californica |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics | Pardosa pseudoannulata | |
0.0429 | - |
acetylthiocholine | pH 8.0, temperature not specified in the publication | Pardosa pseudoannulata | |
0.0616 | - |
acetylthiocholine | pH 7.5, temperature not specified in the publication | Pardosa pseudoannulata | |
0.1986 | - |
butyrylthiocholine | pH 8.0, temperature not specified in the publication | Pardosa pseudoannulata | |
0.2694 | - |
butyrylthiocholine | pH 7.5, temperature not specified in the publication | Pardosa pseudoannulata | |
0.2793 | - |
propionylthiocholine | pH 7.5, temperature not specified in the publication | Pardosa pseudoannulata | |
0.5036 | - |
propionylthiocholine | pH 8.0, temperature not specified in the publication | Pardosa pseudoannulata | |
0.5368 | - |
acetylthiocholine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
0.8588 | - |
butyrylthiocholine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
1.1486 | - |
propionylthiocholine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
1.304 | - |
acetylthiocholine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
1.529 | - |
butyrylthiocholine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
1.548 | - |
propionylthiocholine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
4.414 | - |
acetylthiocholine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
4.496 | - |
propionylthiocholine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
4.542 | - |
butyrylthiocholine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetylcholine + H2O | Tetronarce californica | - |
choline + acetate | - |
? | |
acetylcholine + H2O | Pardosa pseudoannulata | - |
choline + acetate | - |
? | |
acetylcholine + H2O | Tetranychus urticae | - |
choline + acetate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P22303 | - |
- |
Pardosa pseudoannulata | A0A1B1FIV8 | collected from paddy fields of Nanjing (Jiangsu, China) in September 2015 | - |
Pardosa pseudoannulata | A0A1B1FIW0 | collected from paddy fields of Nanjing (Jiangsu, China) in September 2015 | - |
Pardosa pseudoannulata | A0A1B1FIW2 | collected from paddy fields of Nanjing (Jiangsu, China) in September 2015 | - |
Pardosa pseudoannulata | A0A1B1FIZ1 | collected from paddy fields of Nanjing (Jiangsu, China) in September 2015 | - |
Pardosa pseudoannulata | V5QQC6 | collected from paddy fields of Nanjing (Jiangsu, China) in September 2015 | - |
Tetranychus urticae | Q86CZ4 | - |
- |
Tetronarce californica | P04058 | i.e. Tetronarce californica | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.08 | - |
about, crude recombinant enzyme, pH 8.0, temperature not specified in the publication | Pardosa pseudoannulata |
0.1 | - |
about, crude recombinant enzyme, pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata |
0.12 | - |
about, crude recombinant enzyme, pH 7.5, temperature not specified in the publication | Pardosa pseudoannulata |
0.23 | - |
about, crude recombinant enzyme, pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata |
0.315 | - |
crude recombinant enzyme, pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetylcholine + H2O | - |
Tetronarce californica | choline + acetate | - |
? | |
acetylcholine + H2O | - |
Pardosa pseudoannulata | choline + acetate | - |
? | |
acetylcholine + H2O | - |
Tetranychus urticae | choline + acetate | - |
? | |
acetylthiocholine + H2O | - |
Pardosa pseudoannulata | thiocholine + acetate | - |
? | |
acetylthiocholine + H2O | preferred substrate, isozyme PpAChE5 shows the highest catalytic efficiency (Vmax/KM) for substrate acetylthiocholine, which is about 5.4 and 8.6 times compared to butyrylthiocholine and propionylthiocholine, respectively | Pardosa pseudoannulata | thiocholine + acetate | - |
? | |
butyrylthiocholine + H2O | - |
Pardosa pseudoannulata | thiocholine + butyrate | - |
? | |
butyrylthiocholine + H2O | lower activity | Pardosa pseudoannulata | thiocholine + butyrate | - |
? | |
propionylthiocholine + H2O | - |
Pardosa pseudoannulata | thiocholine + propionate | - |
? | |
propionylthiocholine + H2O | low activity | Pardosa pseudoannulata | thiocholine + propionate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AcE1 | - |
Pardosa pseudoannulata |
AcE1 | - |
Tetranychus urticae |
ACE2 | - |
Pardosa pseudoannulata |
ace3 | - |
Pardosa pseudoannulata |
ace4 | - |
Pardosa pseudoannulata |
ace5 | - |
Pardosa pseudoannulata |
AChE | - |
Tetronarce californica |
AChE | - |
Homo sapiens |
AChE | - |
Tetranychus urticae |
AChE1 | - |
Pardosa pseudoannulata |
AChE2 | - |
Pardosa pseudoannulata |
AChE3 | - |
Pardosa pseudoannulata |
AChE4 | - |
Pardosa pseudoannulata |
AChE5 | - |
Tetronarce californica |
hAChE | - |
Homo sapiens |
PpAChE5 | - |
Pardosa pseudoannulata |
TcAChE | - |
Tetronarce californica |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
- |
Pardosa pseudoannulata |
7.5 | - |
- |
Pardosa pseudoannulata |
8 | - |
- |
Pardosa pseudoannulata |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | ligand dissociation constants and inhibition kinetics | Tetronarce californica | |
0.0000736 | - |
BW284c51 | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
0.000245 | - |
eserine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
0.000624 | - |
eserine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
0.00155 | - |
paraoxon | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
0.00164 | - |
diazoxon | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
0.00168 | - |
Carbaryl | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
0.00185 | - |
fenobucarb | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.0000368 | - |
pH 8.0, temperature not specified in the publication | Pardosa pseudoannulata | BW284c51 | |
0.0000512 | - |
pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | BW284c51 | |
0.0000652 | - |
pH 8.0, temperature not specified in the publication | Pardosa pseudoannulata | eserine | |
0.0001167 | - |
pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | eserine | |
0.000471 | - |
pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | BW284c51 | |
0.001163 | - |
pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | eserine | |
0.00186 | - |
pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | eserine | |
0.00254 | - |
pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | BW284c51 | |
0.0217 | - |
pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | iso-ompa |
General Information | Comment | Organism |
---|---|---|
evolution | key amino acid differences at functional sites among AChEs of Torpedo californica, Tetranychus urticae, and Pardosa pseudoannulata, evolutionary relationships, overview | Tetronarce californica |
evolution | key amino acid differences at functional sites among AChEs of Torpedo californica, Tetranychus urticae, and Pardosa pseudoannulata, evolutionary relationships, overview | Pardosa pseudoannulata |
evolution | key amino acid differences at functional sites among AChEs of Torpedo californica, Tetranychus urticae, and Pardosa pseudoannulata, evolutionary relationships, overview | Tetranychus urticae |
additional information | catalysis takes place in a 20-A deep active site gorge and involves a catalytic triad of serine, histidine, and glutamate residues located near the bottom of the gorge, denoted the acylation or A-site. The region near the rim of the gorge has been denoted the peripheral site or P-site | Tetronarce californica |
additional information | catalysis takes place in a 20-A deep active site gorge and involves a catalytic triad of serine, histidine, and glutamate residues located near the bottom of the gorge, denoted the acylation or A-site. The region near the rim of the gorge has been denoted the peripheral site or P-site | Homo sapiens |
additional information | the catalytic triad is formed by residues S200, E327, and H440 | Tetronarce californica |
additional information | the catalytic triad is formed by Ser, Glu, and His residues | Pardosa pseudoannulata |
additional information | the catalytic triad is formed by Ser, Glu, and His residues | Tetranychus urticae |
physiological function | acetylcholinesterase (AChE) is an important neurotransmitter hydrolase in invertebrate and vertebrate nervous systems. The number of AChEs is various among invertebrate species, with different functions including the classical role in terminating synaptic transmission and other non-classical roles | Tetronarce californica |
physiological function | acetylcholinesterase (AChE) is an important neurotransmitter hydrolase in invertebrate and vertebrate nervous systems. The number of AChEs is various among invertebrate species, with different functions including the classical role in terminating synaptic transmission and other non-classical roles | Pardosa pseudoannulata |
physiological function | acetylcholinesterase (AChE) is an important neurotransmitter hydrolase in invertebrate and vertebrate nervous systems. The number of AChEs is various among invertebrate species, with different functions including the classical role in terminating synaptic transmission and other non-classical roles | Tetranychus urticae |