Literature summary for 3.1.1.7 extracted from

Xiao, Q.; Zhou, H.; Wei, H.; Du, H.; Tan, W.; Zhan, Y.; Pistolozzi, M.
A new method to characterize the kinetics of cholinesterases inhibited by carbamates (2017), J. Pharm. Biomed. Anal., 144, 175-182 .

Search for more literature for 3.1.1.7

Inhibitors

Inhibitors	Comment	Organism	Structure
(R)-bambuterol monocarbamate	inhibition kinetics of human acetylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers	Homo sapiens
(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
(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
(S)-bambuterol monocarbamate	inhibition kinetics of human acetylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers	Homo sapiens
(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
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
rac-bambuterol monocarbamate	inhibition kinetics of human acetylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	Michaelis-Menten kinetics	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
acetylcholine + H2O	Homo sapiens	-	choline + acetate	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P22303	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
erythrocyte	-	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acetylcholine + H2O	-	Homo sapiens	choline + acetate	-	?
acetylthiocholine + H2O	-	Homo sapiens	thiocholine + acetate	-	?

Synonyms

Synonyms	Comment	Organism
AChE	-	Homo sapiens
hAChE	-	Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Homo sapiens

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
additional information	-	additional information	inhibition kinetics	Homo sapiens

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Release 2023.1 (January 2023)