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Literature summary extracted from
- A new method to characterize the kinetics of cholinesterases inhibited by carbamates (2017), J. Pharm. Biomed. Anal., 144, 175-182 .
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.1.7 | (R)-bambuterol monocarbamate | inhibition kinetics of human acetylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers | Homo sapiens |  |
| 3.1.1.7 | (R)-[3-[2-(tert-butylamino)-1-hydroxyethyl]-5-(dimethylcarbamoyloxy)phenyl] N,N-dimethylcarbamate | i.e. (R)-bambuterol, inhibition kinetics of human acetylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers | Homo sapiens | |
| 3.1.1.7 | (RS)-[3-[2-(tert-butylamino)-1-hydroxyethyl]-5-(dimethylcarbamoyloxy)phenyl] N,N-dimethylcarbamate | i.e. rac-bambuterol, inhibition kinetics of human acetylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers | Homo sapiens | |
| 3.1.1.7 | (S)-bambuterol monocarbamate | inhibition kinetics of human acetylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers | Homo sapiens | |
| 3.1.1.7 | (S)-[3-[2-(tert-butylamino)-1-hydroxyethyl]-5-(dimethylcarbamoyloxy)phenyl] N,N-dimethylcarbamate | i.e. (S)-bambuterol, inhibition kinetics of human acetylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers | Homo sapiens | |
| 3.1.1.7 | additional information | the inhibition of cholinesterases (ChEs) by carbamates includes a carbamylation (inhibition) step, in which the drug transfers its carbamate moiety to the active site of the enzyme and a decarbamylation (activity recovery) step, in which the carbamyl group is hydrolyzed from the enzyme. The carbamylation and decarbamylation kinetics decide the extent and the duration of the inhibition, thus the full characterization of candidate carbamate inhibitors requires the measurement of the kinetic constants describing both steps. By the analysis of the area under the inhibition-time curve of cholinesterases inhibited by carbamates it is possible to calculate the decarbamylation rate constant from the same data traditionally used to characterize only the carbamylation kinetics, therefore it is possible to obtain a full characterization of the inhibition with a single set of experiments, method validation, a simple and useful approach to reduce the time required for the characterization of carbamate inhibitors, overview | Homo sapiens | |
| 3.1.1.7 | rac-bambuterol monocarbamate | inhibition kinetics of human acetylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers | Homo sapiens | |
| 3.1.1.8 | (R)-bambuterol monocarbamate | inhibition kinetics of human and dog plasma butyrylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers | Canis lupus familiaris | |
| 3.1.1.8 | (R)-bambuterol monocarbamate | inhibition kinetics of human and dog plasma butyrylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers | Homo sapiens | |
| 3.1.1.8 | (R)-[3-[2-(tert-butylamino)-1-hydroxyethyl]-5-(dimethylcarbamoyloxy)phenyl] N,N-dimethylcarbamate | i.e. (R)-bambuterol, inhibition kinetics of human and dog plasma butyrylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers | Canis lupus familiaris | |
| 3.1.1.8 | (R)-[3-[2-(tert-butylamino)-1-hydroxyethyl]-5-(dimethylcarbamoyloxy)phenyl] N,N-dimethylcarbamate | i.e. (R)-bambuterol, inhibition kinetics of human and dog plasma butyrylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers | Homo sapiens | |
| 3.1.1.8 | (RS)-[3-[2-(tert-butylamino)-1-hydroxyethyl]-5-(dimethylcarbamoyloxy)phenyl] N,N-dimethylcarbamate | i.e. rac-bambuterol, inhibition kinetics of human and dog plasma butyrylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers | Canis lupus familiaris | |
| 3.1.1.8 | (RS)-[3-[2-(tert-butylamino)-1-hydroxyethyl]-5-(dimethylcarbamoyloxy)phenyl] N,N-dimethylcarbamate | i.e. rac-bambuterol, inhibition kinetics of human and dog plasma butyrylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers | Homo sapiens | |
| 3.1.1.8 | (S)-bambuterol monocarbamate | inhibition kinetics of human and dog plasma butyrylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers | Canis lupus familiaris | |
| 3.1.1.8 | (S)-bambuterol monocarbamate | inhibition kinetics of human and dog plasma butyrylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers | Homo sapiens | |
| 3.1.1.8 | (S)-[3-[2-(tert-butylamino)-1-hydroxyethyl]-5-(dimethylcarbamoyloxy)phenyl] N,N-dimethylcarbamate | i.e. (S)-bambuterol, inhibition kinetics of human and dog plasma butyrylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers | Canis lupus familiaris | |
| 3.1.1.8 | (S)-[3-[2-(tert-butylamino)-1-hydroxyethyl]-5-(dimethylcarbamoyloxy)phenyl] N,N-dimethylcarbamate | i.e. (S)-bambuterol, inhibition kinetics of human and dog plasma butyrylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers | Homo sapiens | |
| 3.1.1.8 | additional information | the inhibition of cholinesterases (ChEs) by carbamates includes a carbamylation (inhibition) step, in which the drug transfers its carbamate moiety to the active site of the enzyme and a decarbamylation (activity recovery) step, in which the carbamyl group is hydrolyzed from the enzyme. The carbamylation and decarbamylation kinetics decide the extent and the duration of the inhibition, thus the full characterization of candidate carbamate inhibitors requires the measurement of the kinetic constants describing both steps. By the analysis of the area under the inhibition-time curve of cholinesterases inhibited by carbamates it is possible to calculate the decarbamylation rate constant from the same data traditionally used to characterize only the carbamylation kinetics, therefore it is possible to obtain a full characterization of the inhibition with a single set of experiments, method validation, a simple and useful approach to reduce the time required for the characterization of carbamate inhibitors, overview | Canis lupus familiaris | |
| 3.1.1.8 | additional information | the inhibition of cholinesterases (ChEs) by carbamates includes a carbamylation (inhibition) step, in which the drug transfers its carbamate moiety to the active site of the enzyme and a decarbamylation (activity recovery) step, in which the carbamyl group is hydrolyzed from the enzyme. The carbamylation and decarbamylation kinetics decide the extent and the duration of the inhibition, thus the full characterization of candidate carbamate inhibitors requires the measurement of the kinetic constants describing both steps. By the analysis of the area under the inhibition-time curve of cholinesterases inhibited by carbamates it is possible to calculate the decarbamylation rate constant from the same data traditionally used to characterize only the carbamylation kinetics, therefore it is possible to obtain a full characterization of the inhibition with a single set of experiments, method validation, a simple and useful approach to reduce the time required for the characterization of carbamate inhibitors, overview | Homo sapiens | |
| 3.1.1.8 | rac-bambuterol monocarbamate | inhibition kinetics of human and dog plasma butyrylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers | Canis lupus familiaris | |
| 3.1.1.8 | rac-bambuterol monocarbamate | inhibition kinetics of human and dog plasma butyrylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers | 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 | Homo sapiens | |
| 3.1.1.8 | additional information | - |
additional information | Michaelis-Menten kinetics | Homo sapiens | |
| 3.1.1.8 | additional information | - |
additional information | Michaelis-Menten kinetics | Canis lupus familiaris |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.1.7 | acetylcholine + H2O | Homo sapiens | - |
choline + acetate | - |
? | |
| 3.1.1.8 | butyrylcholine + H2O | Homo sapiens | - |
choline + butyrate | - |
? | |
| 3.1.1.8 | butyrylcholine + H2O | Canis lupus familiaris | - |
choline + butyrate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.1.7 | Homo sapiens | P22303 | - |
- |
| 3.1.1.8 | Canis lupus familiaris | P32750 | - |
- |
| 3.1.1.8 | Homo sapiens | P06276 | - |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.1.1.7 | erythrocyte | - |
Homo sapiens | - |
| 3.1.1.8 | blood plasma | - |
Homo sapiens | - |
| 3.1.1.8 | blood plasma | - |
Canis lupus familiaris | - |
| 3.1.1.8 | additional information | BChE is the only cholinesterase in human plasma | Homo sapiens | - |
| 3.1.1.8 | additional information | besides BChE, dog plasma contains also acetylcholinesterase, AChE (EC 3.1.1.7) | Canis lupus familiaris | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.1.7 | acetylcholine + H2O | - |
Homo sapiens | choline + acetate | - |
? | |
| 3.1.1.7 | acetylthiocholine + H2O | - |
Homo sapiens | thiocholine + acetate | - |
? | |
| 3.1.1.8 | (S)-butyrylthiocholine + H2O | - |
Homo sapiens | thiocholine + butyrate | - |
? | |
| 3.1.1.8 | (S)-butyrylthiocholine + H2O | - |
Canis lupus familiaris | thiocholine + butyrate | - |
? | |
| 3.1.1.8 | butyrylcholine + H2O | - |
Homo sapiens | choline + butyrate | - |
? | |
| 3.1.1.8 | butyrylcholine + H2O | - |
Canis lupus familiaris | choline + butyrate | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.1.7 | AChE | - |
Homo sapiens |
| 3.1.1.7 | hAChE | - |
Homo sapiens |
| 3.1.1.8 | BChE | - |
Homo sapiens |
| 3.1.1.8 | BChE | - |
Canis lupus familiaris |
| 3.1.1.8 | butyrylcholinesterase | - |
Homo sapiens |
| 3.1.1.8 | butyrylcholinesterase | - |
Canis lupus familiaris |
| 3.1.1.8 | dBChE | - |
Canis lupus familiaris |
| 3.1.1.8 | hBChE | - |
Homo sapiens |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.7 | 37 | - |
assay at | Homo sapiens |
| 3.1.1.8 | 37 | - |
assay at | Homo sapiens |
| 3.1.1.8 | 37 | - |
assay at | Canis lupus familiaris |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.7 | 8 | - |
assay at | Homo sapiens |
| 3.1.1.8 | 8 | - |
assay at | Homo sapiens |
| 3.1.1.8 | 8 | - |
assay at | Canis lupus familiaris |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.1.7 | additional information | - |
additional information | inhibition kinetics | Homo sapiens | |
| 3.1.1.8 | additional information | - |
additional information | inhibition kinetics | Homo sapiens | |
| 3.1.1.8 | additional information | - |
additional information | inhibition kinetics | Canis lupus familiaris |
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