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An analysis of acetylcholinesterase sequence for predicting mechanisms of its non-catalytic actions

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Author(s): Malathi Srivatsan

Journal: Bioinformation
ISSN 0973-2063

Volume: 1;
Issue: 8;
Start page: 281;
Date: 2006;
Original page

Keywords: motifs | domain | finger prints

ABSTRACT
The enzyme acetylcholinesterase (AChE) which belongs to the family of α/β hydrolases is well known for hydrolyzing the neurotransmitter acetylcholine (ACh). In addition to its catalytic function, AChE appears to play a significant non-catalytic role in development, regeneration and modulation of properties of neurons. However the mechanisms underlying these important actions of AChE are unknown. It prompted the analysis of the sequence of fetal bovine serum AChE to seek clue(s) for the mechanisms of AChE non-catalytic actions. The searches for motifs, finger prints and domains demonstrated the presence of a highly conserved carboxylesterase type B signature in AChE from slime molds to human. Interestingly, the presence of finger prints for a metabotropic glutamate receptor, gap junction protein connexin, a calcium binding motif, several phosphorylation sites, and a motif similar to nicotinic acetylcholine receptor were also found in the sequence of AChE suggesting a role for AChE in cell signalling. The similarity search using gapped BLAST retrieved previously known similar proteins, namely neurotactin, neuroligin and thyroglobulin. When aligned neurotactin, neuroligin and bovine AChE showed the presence of three stretches of consensus, one of which is carboxylesterase B signature. The identity of the other two are not known. Amino acids in these stretches in AChE may be involved in possible growth factor like action and awaits experimental verification. Thus sequence analysis can be very useful for biologists while searching for a possible mechanism of action of a protein. Further, these results underscore the significance of performing both local and global searches to identify possible functional domains as well as consensus sequence.
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