Wiesner_2007_J.Enzyme.Inhib.Med.Chem_22_417

Reference

Title : Acetylcholinesterases--the structural similarities and differences - Wiesner_2007_J.Enzyme.Inhib.Med.Chem_22_417
Author(s) : Wiesner J , Kriz Z , Kuca K , Jun D , Koca J
Ref : J Enzyme Inhib Med Chem , 22 :417 , 2007
Abstract :

Acetylcholinesterase (AChE) is a widely spread enzyme playing a very important role in nerve signal transmission. As AChE controls key processes, its inhibition leads to the very fast death of an organism, including humans. However, when this feature is to be used for killing of unwanted organisms (i.e. mosquitoes), one is faced with the question - how much do AChEs differ between species and what are the differences? Here, a theoretical point of view was utilized to identify the structural basis for such differences. The various primary and tertiary alignments show that AChEs are very evolutionary conserved enzymes and this fact could lead to difficulties, for example, in the search for inhibitors specific for a particular species.

PubMedSearch : Wiesner_2007_J.Enzyme.Inhib.Med.Chem_22_417
PubMedID: 17847707

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Citations formats

Wiesner J, Kriz Z, Kuca K, Jun D, Koca J (2007)
Acetylcholinesterases--the structural similarities and differences
J Enzyme Inhib Med Chem 22 :417

Wiesner J, Kriz Z, Kuca K, Jun D, Koca J (2007)
J Enzyme Inhib Med Chem 22 :417