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Literature summary for 3.1.1.8 extracted from

  • Zdrazilova, P.; Stepankova, S.; Komersova, A.; Vranova, M.; Komers, K.; Cegan, A.
    Kinetics of 13 new cholinesterase inhibitors (2006), Z. Naturforsch. C, 61, 611-617.
    View publication on PubMed
Search for more literature for 3.1.1.8

Inhibitors

Inhibitors Comment Organism Structure
2-chlorophenyl 1,2-dimethylhydrazinecarboxylate
-
 Equus caballus
2-chlorophenyl 1-methylhydrazinecarboxylate
-
 Equus caballus
3-chlorophenyl 1,2-dimethylhydrazinecarboxylate
-
 Equus caballus
3-chlorophenyl 1-methylhydrazinecarboxylate
-
 Equus caballus
3-N,N-diethylaminophenyl-N'-(1-alkyl) carbamates inhibit quickly by carbamoylation Equus caballus
3-N,N-diethylaminophenyl-N'-(1-butyl) carbamate
-
 Equus caballus
3-N,N-diethylaminophenyl-N'-(1-ethyl) carbamate
-
 Equus caballus
3-N,N-diethylaminophenyl-N'-(1-hexyl) carbamate
-
 Equus caballus
3-N,N-diethylaminophenyl-N'-(1-octyl) carbamate
-
 Equus caballus
3-N,N-diethylaminophenyl-N'-(1-propyl) carbamate
-
 Equus caballus
4-chlorophenyl 1,2-dimethylhydrazinecarboxylate
-
 Equus caballus
4-chlorophenyl 1-methylhydrazinecarboxylate
-
 Equus caballus
galantamin
-
 Equus caballus
additional information some inhibitors fullfill the competitive inhibition model with irreversible reaction between enzyme and inhibitor, but e.g. not galantamin Equus caballus
phenyl 1,2-dimethylhydrazinecarboxylate
-
 Equus caballus
phenyl 1-methylhydrazinecarboxylate
-
 Equus caballus
rivastigmin
-
 Equus caballus
sevin
-
 Equus caballus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Equus caballus
-
-

Organism

Organism UniProt Comment Textmining
Equus caballus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
blood plasma
-
 Equus caballus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.5
-
-
 Equus caballus

Synonyms

Synonyms Comment Organism
BChE
-
 Equus caballus
butyrylcholinesterase
-
 Equus caballus
cholinesterase
-
 Equus caballus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Equus caballus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Equus caballus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information inhibition kinetics, value of carbamoylation inhibition Equus caballus