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Literature summary extracted from
- Design, synthesis and cellular characterization of a dual inhibitor of 5-lipoxygenase and soluble epoxide hydrolase (2016), Molecules, 22, 45.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.1.7 | gene ace1, sequence comparisons and phylogenetic analysis | Tetranychus urticae |
| 3.1.1.7 | gene ace1, sequence comparisons and phylogenetic analysis, recombinant expression of isozyme PpAChE1 in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system | Pardosa pseudoannulata |
| 3.1.1.7 | gene ace2, sequence comparisons and phylogenetic analysis, recombinant expression of isozyme PpAChE2 in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system | Pardosa pseudoannulata |
| 3.1.1.7 | gene ace3, sequence comparisons and phylogenetic analysis, recombinant expression of isozyme PpAChE3 in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system | Pardosa pseudoannulata |
| 3.1.1.7 | gene ace4, sequence comparisons and phylogenetic analysis, recombinant expression of isozyme PpAChE4 in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system | Pardosa pseudoannulata |
| 3.1.1.7 | 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 |
| 3.1.1.7 | gene ache, sequence comparisons and phylogenetic analysis | Tetronarce californica |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.1.1.7 | analysis of crystal structure PDB ID 4ey4 | Tetronarce californica |
| 3.1.1.7 | analysis of crystal structure PDB ID 4ey4 | Homo sapiens |
| 3.1.1.8 | purified enzyme human BChE in complex with the reversible ligands, decamethonium, thioflavin T, propidium, huprine, and ethopropazine, crystals of the BChES2-propidium complex were grown by cocrystallization in the presence of 1 mM ligand. The structure of the complex is solved at 3.0 A resolution, the structure of enzyme-decamethonium is solved at 2.3 A resolution, crystals of the BChECHO-ethopropazine complex are grown by cocrystallization in the presence of 1 mM ligand, the structure is solved at 2.35 A resolution | Homo sapiens |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.13.11.34 | 1-(3-[5-(hydroxyureido)methyl-2-methoxyphenoxy]propyl)-3-[4-(trifluoromethoxy)phenyl]urea | KM55, a multitarget ligand and dual 5-lipoxygenase (5-LO)/soluble epoxide hydrolase (sEH) inhibitor. KM55 potently inhibits both enzymes in vitro and attenuates the formation of leukotrienes in human whole blood. It significantly inhibits the LPS-induced adhesion of leukocytes to endothelial cells by blocking leukocyte activation. Compound synthesis and evaluation, overview. KM55 inhibits the formation of leukotriene B4 and 5-hydroxyeicosatrienoic acid, while the formation of 12-hydroperoxyicosatetraenoate and 15-hydroperoxyicosatetraenoate are unaffected. KM55 blocks leukocyte-endothelial cell interaction by impairing leukocyte activation, whereas endothelial cells are not affected | Homo sapiens |  |
| 1.13.11.34 | zileuton | - |
Homo sapiens | |
| 3.1.1.7 | (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 | |
| 3.1.1.7 | (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 | |
| 3.1.1.7 | (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 | |
| 3.1.1.7 | (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 | |
| 3.1.1.7 | 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 | |
| 3.1.1.7 | Carbaryl | - |
Pardosa pseudoannulata | |
| 3.1.1.7 | 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 | |
| 3.1.1.7 | 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 | |
| 3.1.1.7 | diazoxon | - |
Pardosa pseudoannulata | |
| 3.1.1.7 | edrophonium | - |
Homo sapiens | |
| 3.1.1.7 | edrophonium | - |
Tetronarce californica | |
| 3.1.1.7 | eserine | - |
Pardosa pseudoannulata | |
| 3.1.1.7 | 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 | |
| 3.1.1.7 | ethopropazine | - |
Tetronarce californica | |
| 3.1.1.7 | fenobucarb | - |
Pardosa pseudoannulata | |
| 3.1.1.7 | iso-ompa | tetraisopropyl diphosphoramide, inhibition of activity with butyrylthiocholine | Pardosa pseudoannulata | |
| 3.1.1.7 | additional information | determination and analysis of the crystal structures of enzyme-bound ligands | Homo sapiens | |
| 3.1.1.7 | 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 | |
| 3.1.1.7 | additional information | determination and analysis of the crystal structures of enzyme-bound ligands | Tetronarce californica | |
| 3.1.1.7 | paraoxon | - |
Pardosa pseudoannulata | |
| 3.1.1.7 | propidium | - |
Homo sapiens | |
| 3.1.1.7 | propidium | structure of the complex is solved at 3.0 A resolution, absence involving Trp279 in TcAChE at the gorge | Tetronarce californica | |
| 3.1.1.7 | thioflavin T | - |
Homo sapiens | |
| 3.1.1.7 | 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 | |
| 3.1.1.8 | (7R,11R)-huprine 19 | binding structure from analysis of the crystal structure | Homo sapiens | |
| 3.1.1.8 | (7S,11S)-huprine W | binding structure from analysis of the crystal structure | Homo sapiens | |
| 3.1.1.8 | decamethonium | binding structure from analysis of the crystal structure determined at 2.3 A resolution, overview. Decamethonium spans the gorge of BChE | Homo sapiens | |
| 3.1.1.8 | edrophonium | lower inhibition | Homo sapiens | |
| 3.1.1.8 | ethopropazine | ethopropazine is a substituted phenothiazine with a marked specificity for BChE. The 9000fold difference in Ki between hAChE and hBChE reflects this specificity, structure from analysis of the crystal structure determined at 2.35 A resolution, overview | Homo sapiens | |
| 3.1.1.8 | additional information | determination and analysis of the crystal structures of enzyme-bound ligands | Homo sapiens | |
| 3.1.1.8 | propidium | propidium binds very differently to BChE and mostlly fills the gorge due to absence of a blocking Trp residue. The phenanthridinium ring is slotted into the groove of the acyl-binding pocket, with the amino group at interaction distance from Trp231 (2.8 A to the center of the 6-carbon ring) and Ser198-O (3.3 A), and T-stacked to Phe329. The alkyldiethylmethylammonium moiety extends to Trp82 of the A-site at cation-Pi interaction distance (3.1 A between the 6-carbon ring indole center and C5). The second ethyl group of the quaternary center docks against the propidium phenyl group (4 A to aromatic plane), suggesting an intramolecular cation-Pi interaction. The propidium phenyl group is oriented toward the P-site residues Tyr332 and Asp70 | Homo sapiens | |
| 3.1.1.8 | thioflavin T | binding structure from analysis of the crystal structure, PDB ID 6ESY, inhibition kinetics and thermodynamics, overview | Homo sapiens | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.1.7 | additional information | - |
additional information | Michaelis-Menten kinetics | Pardosa pseudoannulata | |
| 3.1.1.7 | 0.0429 | - |
acetylthiocholine | pH 8.0, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.7 | 0.0616 | - |
acetylthiocholine | pH 7.5, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.7 | 0.1986 | - |
butyrylthiocholine | pH 8.0, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.7 | 0.2694 | - |
butyrylthiocholine | pH 7.5, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.7 | 0.2793 | - |
propionylthiocholine | pH 7.5, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.7 | 0.5036 | - |
propionylthiocholine | pH 8.0, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.7 | 0.5368 | - |
acetylthiocholine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.7 | 0.8588 | - |
butyrylthiocholine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.7 | 1.1486 | - |
propionylthiocholine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.7 | 1.304 | - |
acetylthiocholine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.7 | 1.529 | - |
butyrylthiocholine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.7 | 1.548 | - |
propionylthiocholine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.7 | 4.414 | - |
acetylthiocholine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.7 | 4.496 | - |
propionylthiocholine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.7 | 4.542 | - |
butyrylthiocholine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.11.34 | arachidonate + O2 | Homo sapiens | - |
(5S,6S,7E,9E,11Z,14Z)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O | - |
? | |
| 3.1.1.7 | acetylcholine + H2O | Tetronarce californica | - |
choline + acetate | - |
? | |
| 3.1.1.7 | acetylcholine + H2O | Pardosa pseudoannulata | - |
choline + acetate | - |
? | |
| 3.1.1.7 | acetylcholine + H2O | Tetranychus urticae | - |
choline + acetate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.13.11.34 | Homo sapiens | P09917 | - |
- |
| 3.1.1.7 | Homo sapiens | P22303 | - |
- |
| 3.1.1.7 | Pardosa pseudoannulata | A0A1B1FIV8 | collected from paddy fields of Nanjing (Jiangsu, China) in September 2015 | - |
| 3.1.1.7 | Pardosa pseudoannulata | A0A1B1FIW0 | collected from paddy fields of Nanjing (Jiangsu, China) in September 2015 | - |
| 3.1.1.7 | Pardosa pseudoannulata | A0A1B1FIW2 | collected from paddy fields of Nanjing (Jiangsu, China) in September 2015 | - |
| 3.1.1.7 | Pardosa pseudoannulata | A0A1B1FIZ1 | collected from paddy fields of Nanjing (Jiangsu, China) in September 2015 | - |
| 3.1.1.7 | Pardosa pseudoannulata | V5QQC6 | collected from paddy fields of Nanjing (Jiangsu, China) in September 2015 | - |
| 3.1.1.7 | Tetranychus urticae | Q86CZ4 | - |
- |
| 3.1.1.7 | Tetronarce californica | P04058 | i.e. Tetronarce californica | - |
| 3.1.1.8 | Homo sapiens | P06276 | - |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.13.11.34 | endothelial cell | - |
Homo sapiens | - |
| 1.13.11.34 | endothelial cell | primary | Homo sapiens | - |
| 1.13.11.34 | leukocyte | - |
Homo sapiens | - |
| 1.13.11.34 | THP-1 cell | - |
Homo sapiens | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.7 | 0.08 | - |
about, crude recombinant enzyme, pH 8.0, temperature not specified in the publication | Pardosa pseudoannulata |
| 3.1.1.7 | 0.1 | - |
about, crude recombinant enzyme, pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata |
| 3.1.1.7 | 0.12 | - |
about, crude recombinant enzyme, pH 7.5, temperature not specified in the publication | Pardosa pseudoannulata |
| 3.1.1.7 | 0.23 | - |
about, crude recombinant enzyme, pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata |
| 3.1.1.7 | 0.315 | - |
crude recombinant enzyme, pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.11.34 | arachidonate + O2 | - |
Homo sapiens | (5S,6S,7E,9E,11Z,14Z)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O | - |
? | |
| 3.1.1.7 | acetylcholine + H2O | - |
Tetronarce californica | choline + acetate | - |
? | |
| 3.1.1.7 | acetylcholine + H2O | - |
Pardosa pseudoannulata | choline + acetate | - |
? | |
| 3.1.1.7 | acetylcholine + H2O | - |
Tetranychus urticae | choline + acetate | - |
? | |
| 3.1.1.7 | acetylthiocholine + H2O | - |
Pardosa pseudoannulata | thiocholine + acetate | - |
? | |
| 3.1.1.7 | 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 | - |
? | |
| 3.1.1.7 | butyrylthiocholine + H2O | - |
Pardosa pseudoannulata | thiocholine + butyrate | - |
? | |
| 3.1.1.7 | butyrylthiocholine + H2O | lower activity | Pardosa pseudoannulata | thiocholine + butyrate | - |
? | |
| 3.1.1.7 | propionylthiocholine + H2O | - |
Pardosa pseudoannulata | thiocholine + propionate | - |
? | |
| 3.1.1.7 | propionylthiocholine + H2O | low activity | Pardosa pseudoannulata | thiocholine + propionate | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.13.11.34 | 5-lipoxygenase | - |
Homo sapiens |
| 1.13.11.34 | 5-LO | - |
Homo sapiens |
| 3.1.1.7 | AcE1 | - |
Pardosa pseudoannulata |
| 3.1.1.7 | AcE1 | - |
Tetranychus urticae |
| 3.1.1.7 | ACE2 | - |
Pardosa pseudoannulata |
| 3.1.1.7 | ace3 | - |
Pardosa pseudoannulata |
| 3.1.1.7 | ace4 | - |
Pardosa pseudoannulata |
| 3.1.1.7 | ace5 | - |
Pardosa pseudoannulata |
| 3.1.1.7 | AChE | - |
Tetronarce californica |
| 3.1.1.7 | AChE | - |
Homo sapiens |
| 3.1.1.7 | AChE | - |
Tetranychus urticae |
| 3.1.1.7 | AChE1 | - |
Pardosa pseudoannulata |
| 3.1.1.7 | AChE2 | - |
Pardosa pseudoannulata |
| 3.1.1.7 | AChE3 | - |
Pardosa pseudoannulata |
| 3.1.1.7 | AChE4 | - |
Pardosa pseudoannulata |
| 3.1.1.7 | AChE5 | - |
Tetronarce californica |
| 3.1.1.7 | hAChE | - |
Homo sapiens |
| 3.1.1.7 | PpAChE5 | - |
Pardosa pseudoannulata |
| 3.1.1.7 | TcAChE | - |
Tetronarce californica |
| 3.1.1.8 | hBChE | - |
Homo sapiens |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.34 | 37 | - |
assay at | Homo sapiens |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.34 | 7.4 | - |
assay at | Homo sapiens |
| 3.1.1.7 | 7 | - |
- |
Pardosa pseudoannulata |
| 3.1.1.7 | 7.5 | - |
- |
Pardosa pseudoannulata |
| 3.1.1.7 | 8 | - |
- |
Pardosa pseudoannulata |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.1.7 | additional information | - |
additional information | ligand dissociation constants and inhibition kinetics | Tetronarce californica | |
| 3.1.1.7 | 0.0000736 | - |
BW284c51 | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.7 | 0.000245 | - |
eserine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.7 | 0.000624 | - |
eserine | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.7 | 0.00155 | - |
paraoxon | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.7 | 0.00164 | - |
diazoxon | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.7 | 0.00168 | - |
Carbaryl | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.7 | 0.00185 | - |
fenobucarb | pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | |
| 3.1.1.8 | additional information | - |
additional information | ligand dissociation constants and inhibition kinetics | Homo sapiens | |
| 3.1.1.8 | 0.00043 | - |
propidium | pH and temperature not specified in the publication | Homo sapiens | |
| 3.1.1.8 | 0.0008 | - |
thioflavin T | pH and temperature not specified in the publication | Homo sapiens | |
| 3.1.1.8 | 0.0045 | - |
decamethonium | pH and temperature not specified in the publication | Homo sapiens | |
| 3.1.1.8 | 0.049 | - |
edrophonium | pH and temperature not specified in the publication | Homo sapiens | |
IC50 Value
| EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|---|
| 1.13.11.34 | 0.0013 | - |
pH 7.4, 37°C | Homo sapiens | 1-(3-[5-(hydroxyureido)methyl-2-methoxyphenoxy]propyl)-3-[4-(trifluoromethoxy)phenyl]urea | |
| 3.1.1.7 | 0.0000368 | - |
pH 8.0, temperature not specified in the publication | Pardosa pseudoannulata | BW284c51 | |
| 3.1.1.7 | 0.0000512 | - |
pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | BW284c51 | |
| 3.1.1.7 | 0.0000652 | - |
pH 8.0, temperature not specified in the publication | Pardosa pseudoannulata | eserine | |
| 3.1.1.7 | 0.0001167 | - |
pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | eserine | |
| 3.1.1.7 | 0.000471 | - |
pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | BW284c51 | |
| 3.1.1.7 | 0.001163 | - |
pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | eserine | |
| 3.1.1.7 | 0.00186 | - |
pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | eserine | |
| 3.1.1.7 | 0.00254 | - |
pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | BW284c51 | |
| 3.1.1.7 | 0.0217 | - |
pH 7.0, temperature not specified in the publication | Pardosa pseudoannulata | iso-ompa | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.1.1.7 | evolution | key amino acid differences at functional sites among AChEs of Torpedo californica, Tetranychus urticae, and Pardosa pseudoannulata, evolutionary relationships, overview | Tetronarce californica |
| 3.1.1.7 | evolution | key amino acid differences at functional sites among AChEs of Torpedo californica, Tetranychus urticae, and Pardosa pseudoannulata, evolutionary relationships, overview | Pardosa pseudoannulata |
| 3.1.1.7 | evolution | key amino acid differences at functional sites among AChEs of Torpedo californica, Tetranychus urticae, and Pardosa pseudoannulata, evolutionary relationships, overview | Tetranychus urticae |
| 3.1.1.7 | 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 |
| 3.1.1.7 | 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 |
| 3.1.1.7 | additional information | the catalytic triad is formed by residues S200, E327, and H440 | Tetronarce californica |
| 3.1.1.7 | additional information | the catalytic triad is formed by Ser, Glu, and His residues | Pardosa pseudoannulata |
| 3.1.1.7 | additional information | the catalytic triad is formed by Ser, Glu, and His residues | Tetranychus urticae |
| 3.1.1.7 | 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 |
| 3.1.1.7 | 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 |
| 3.1.1.7 | 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 |
| 3.1.1.8 | 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 |
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Release 2023.1 (January 2023)
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