Literature summary for 3.1.1.7 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.

Search for more literature for 3.1.1.7

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-
Rattus norvegicus	-	-	-
Sus scrofa	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
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
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
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

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)