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Literature summary extracted from

  • Darvesh, S.; Darvesh, K.V.; McDonald, R.S.; Mataija, D.; Walsh, R.; Mothana, S.; Lockridge, O.; Martin, E.
    Carbamates with differential mechanism of inhibition toward acetylcholinesterase and butyrylcholinesterase (2008), J. Med. Chem., 51, 4200-4212.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.8 A328F the mutant is more sensitive to aryl phenothiazine carbamate inhibitors and deactivation, i.e. 4-biphenyl phenothiazine carbamate, compared to the wild-type enzyme Homo sapiens
3.1.1.8 A328W the mutant is more sensitive to aryl phenothiazine carbamate inhibitors and deactivation, i.e. 4-biphenyl phenothiazine carbamate, compared to the wild-type enzyme Homo sapiens
3.1.1.8 A328Y the mutant is more sensitive to aryl phenothiazine carbamate inhibitors and deactivation, i.e. 4-biphenyl phenothiazine carbamate, compared to the wild-type enzyme Homo sapiens
3.1.1.8 A539T the mutant is more sensitive to aryl phenothiazine carbamate inhibitors and deactivation, i.e. 4-biphenyl phenothiazine carbamate, compared to the wild-type enzyme Homo sapiens
3.1.1.8 D70G the mutant is more sensitive to aryl phenothiazine carbamate inhibitors and deactivation, i.e. 4-biphenyl phenothiazine carbamate, compared to the wild-type enzyme Homo sapiens
3.1.1.8 F329A the mutant is more sensitive to aryl phenothiazine carbamate inhibitors and deactivation, i.e. 4-biphenyl phenothiazine carbamate, compared to the wild-type enzyme Homo sapiens
3.1.1.8 Y332A the mutant is more sensitive to aryl phenothiazine carbamate inhibitors and deactivation, i.e. 4-biphenyl phenothiazine carbamate, compared to the wild-type enzyme Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.7 1-naphthyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 2-(1-piperidinyl)ethyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 2-(1-pyrrolidinyl)ethyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 2-(4-morpholino)ethyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 2-(N,N-diethylamino)ethyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 2-(N,N-dimethylamino)ethyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 2-chlorophenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 2-methoxyphenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 2-methylphenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 2-naphthyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 2-t-butylphenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 3-(N,N-diethylamino)propyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 3-(N,N-dimethylamino) phenyl phenothiazine carbamate binding by residues F329 and Y332, structure, overview Homo sapiens
3.1.1.7 3-chlorophenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 3-methoxyphenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 3-methylphenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 4-biphenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 4-chlorophenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 4-methoxyphenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 4-methylphenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 4-t-butylphenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 butyl carbamate
-
 Homo sapiens
3.1.1.7 cyclopentyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 donepezil
-
 Homo sapiens
3.1.1.7 ethyl carbamate
-
 Homo sapiens
3.1.1.7 galanthamine
-
 Homo sapiens
3.1.1.7 additional information inhibitor molecular mechanics calculations, general mechanism of pseudoirreversible cholinesterase inhibition by carbamates. Enzyme deactivation is initiated by nucleophilic attack of the catalytic triad serine oxygen on the carbonyl group of the carbamate, structure-activity relationships, overview Homo sapiens
3.1.1.7 phenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 propyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.7 rivastigmine
-
 Homo sapiens
3.1.1.7 t-butyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 1-naphthyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 2-(1-piperidinyl)ethyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 2-(1-pyrrolidinyl)ethyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 2-(4-morpholino)ethyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 2-(diethylamino)ethyl 10H-phenothiazine-10-carboxylate
-
 Homo sapiens
3.1.1.8 2-(dimethylamino)ethyl 10H-phenothiazine-10-carboxylate
-
 Homo sapiens
3.1.1.8 2-chlorophenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 2-methoxyphenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 2-methylphenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 2-naphthyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 2-t-butylphenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 3-(diethylamino)propyl 10H-phenothiazine-10-carboxylate
-
 Homo sapiens
3.1.1.8 3-(N,N-dimethylamino) phenyl phenothiazine carbamate binding by residues F329 and Y332, structure, overview Homo sapiens
3.1.1.8 3-chlorophenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 3-methoxyphenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 3-methylphenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 4-biphenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 4-chlorophenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 4-methoxyphenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 4-methylphenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 4-t-butylphenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 butyl carbamate
-
 Homo sapiens
3.1.1.8 cyclopentyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 donepezil
-
 Homo sapiens
3.1.1.8 ethyl carbamate
-
 Homo sapiens
3.1.1.8 galanthamine
-
 Homo sapiens
3.1.1.8 iso-propyl carbamate
-
 Homo sapiens
3.1.1.8 methyl carbamate
-
 Homo sapiens
3.1.1.8 additional information inhibitor molecular mechanics calculations, general mechanism of pseudoirreversible cholinesterase inhibition by carbamates. Enzyme deactivation is initiated by nucleophilic attack of the catalytic triad serine oxygen on the carbonyl group of the carbamate, structure-activity relationships of wild-type and mutant enzymes, overview Homo sapiens
3.1.1.8 phenyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 propyl phenothiazine carbamate
-
 Homo sapiens
3.1.1.8 rivastigmine
-
 Homo sapiens
3.1.1.8 tert-butyl 10H-phenothiazine-10-carboxylate
-
 Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.8 extracellular
-
 Homo sapiens
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.1.7 additional information Homo sapiens acetylcholinesterase is a serine hydrolase that catalyze the hydrolysis of acetylcholine, thus regulating cholinergic neurotransmission ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.7 Homo sapiens
-
-
-
3.1.1.8 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.8 plasma
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.7 acetylthiocholine + H2O detection using 5,5'-dithiobis(2-nitrobenzoic acid) Homo sapiens acetate + thiocholine
-
 ?
3.1.1.7 additional information acetylcholinesterase is a serine hydrolase that catalyze the hydrolysis of acetylcholine, thus regulating cholinergic neurotransmission Homo sapiens ?
-
 ?
3.1.1.8 butyrylthiocholine + H2O detection using 5,5'-dithiobis(2-nitrobenzoic acid) Homo sapiens butyrate + thiocholine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.7 acetylcholinesterase
-
 Homo sapiens
3.1.1.7 AChE
-
 Homo sapiens
3.1.1.8 BuChE
-
 Homo sapiens
3.1.1.8 butyrylcholinesterase
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.8 23
-
 assay at Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.1.1.7 additional information
-
 additional information molecular mechanics calculations and inhibition kinetics, overview Homo sapiens
3.1.1.8 additional information
-
 additional information molecular mechanics calculations and inhibition kinetics, overview Homo sapiens
3.1.1.8 0.0006
-
 2-(diethylamino)ethyl 10H-phenothiazine-10-carboxylate 23°C Homo sapiens
3.1.1.8 0.00065
-
 2-(1-pyrrolidinyl)ethyl phenothiazine carbamate 23°C Homo sapiens
3.1.1.8 0.00074
-
 3-(diethylamino)propyl 10H-phenothiazine-10-carboxylate 23°C Homo sapiens
3.1.1.8 0.0024
-
 2-(4-morpholino)ethyl phenothiazine carbamate 23°C Homo sapiens
3.1.1.8 0.0025
-
 2-(dimethylamino)ethyl 10H-phenothiazine-10-carboxylate 23°C Homo sapiens
3.1.1.8 0.0032
-
 2-(1-piperidinyl)ethyl phenothiazine carbamate 23°C Homo sapiens
3.1.1.8 0.0032
-
 cyclopentyl phenothiazine carbamate 23°C Homo sapiens
3.1.1.8 0.0043
-
 tert-butyl 10H-phenothiazine-10-carboxylate 23°C Homo sapiens
3.1.1.8 0.0102
-
 methyl carbamate 23°C Homo sapiens
3.1.1.8 0.0134
-
 n-butyl carbamate 23°C Homo sapiens
3.1.1.8 0.0181
-
 iso-propyl carbamate 23°C Homo sapiens
3.1.1.8 0.0234
-
 ethyl carbamate 23°C Homo sapiens
3.1.1.8 0.26
-
 propyl phenothiazine carbamate 23°C Homo sapiens