Crystallization (Comment) | Organism |
---|---|
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 | Comment | Organism | Structure |
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(7R,11R)-huprine 19 | binding structure from analysis of the crystal structure | Homo sapiens | |
(7S,11S)-huprine W | binding structure from analysis of the crystal structure | Homo sapiens | |
decamethonium | binding structure from analysis of the crystal structure determined at 2.3 A resolution, overview. Decamethonium spans the gorge of BChE | Homo sapiens | |
edrophonium | lower inhibition | Homo sapiens | |
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 | |
additional information | determination and analysis of the crystal structures of enzyme-bound ligands | Homo sapiens | |
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 | |
thioflavin T | binding structure from analysis of the crystal structure, PDB ID 6ESY, inhibition kinetics and thermodynamics, overview | Homo sapiens |
Organism | UniProt | Comment | Textmining |
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Homo sapiens | P06276 | - |
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Synonyms | Comment | Organism |
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hBChE | - |
Homo sapiens |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | ligand dissociation constants and inhibition kinetics | Homo sapiens | |
0.00043 | - |
propidium | pH and temperature not specified in the publication | Homo sapiens | |
0.0008 | - |
thioflavin T | pH and temperature not specified in the publication | Homo sapiens | |
0.0045 | - |
decamethonium | pH and temperature not specified in the publication | Homo sapiens | |
0.049 | - |
edrophonium | pH and temperature not specified in the publication | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
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 |