Literature summary extracted from

Kuca, K.; Cabal, J.; Kassa, J.
In vitro reactivation of sarin-inhibited brain acetylcholinesterase from different species by various oximes (2005), J. Enzyme Inhib. Med. Chem., 20, 227-232.

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.1.1.7	Homo sapiens	-	-	-
3.1.1.7	Rattus norvegicus	-	-	-
3.1.1.7	Sus scrofa	-	-	-

Renatured (Commentary)

EC Number	Renatured (Comment)	Organism
3.1.1.7	analysis of reactivation of enzyme by various oximes after inhibition by sarin. Comparison of human, pig and rat enzyme. Higher affinity of oximes 1,1'-butane-1,4-diylbis(2-((Z)-(hydroxyimino)methyl)pyridinium),i.e. K033, and 4-(aminocarbonyl)-1-(((2-((Z)-(hydroxyimino)methyl)pyridinium-1-yl)methoxy)methyl)pyridinium dichloride, i.e. HI-6, for the intact enzymes than obidoxime and pralidoxime	Rattus norvegicus
3.1.1.7	analysis of reactivation of enzyme by various oximes after inhibition by sarin. Comparison of human, pig and rat enzyme. Higher affinity of oximes K033 and HI-6 for the intact enzymes than obidoxime and pralidoxime	Sus scrofa
3.1.1.7	analysis of reactivation of enzyme by various oximes after inhibition by sarin. Comparison of human, pig and rat enzyme. Higher affinity of oximes K033 and HI-6 for the intact enzymes than obidoxime and pralidoxime. Markedly low affinity of obidoxime to human enzyme	Homo sapiens

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
3.1.1.7	brain	-	Homo sapiens	-
3.1.1.7	brain	-	Rattus norvegicus	-
3.1.1.7	brain	-	Sus scrofa	-

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Release 2023.1 (January 2023)