Acetylcholinesterases--the structural similarities and differences
Language English Country England, Great Britain Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Acetylcholinesterase chemistry MeSH
- Drosophila melanogaster metabolism MeSH
- Protein Conformation MeSH
- Conserved Sequence MeSH
- Humans MeSH
- Evolution, Molecular MeSH
- Molecular Conformation MeSH
- Molecular Sequence Data MeSH
- Mice MeSH
- Protein Folding MeSH
- Amino Acid Sequence MeSH
- Sequence Homology, Amino Acid MeSH
- Signal Transduction MeSH
- Binding Sites MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Acetylcholinesterase MeSH
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.
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