Acetylcholinesterases--the structural similarities and differences.
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.
Wiesner
Jirí
J
National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5/A4, 625 00 Brno, Czech Republic.
Kriz
Zdenek
Z
Kuca
Kamil
K
Jun
Daniel
D
Koca
Jaroslav
J
D000110:Acetylcholinesterase / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D017124:Conserved Sequence; D004331:Drosophila melanogaster / Q000378:metabolism; D019143:Evolution, Molecular; D006801:Humans; D051379:Mice; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction
D000110:Acetylcholinesterase