Abstract
Objective: Computational studies on fish brain acetylcholinesterase were conducted, expanding our views and for a deeper understanding of the activity of the fish acetylcholinesterase enzyme.
 Methods: Physico-chemical properties of the fish acetylcholinesterase enzyme were studied. Homology model of the acetylcholinesterase enzyme was predicted, validated its quality and active sites were predicted. The amino acid frequency in the active sites was also compared. Similarly, the secondary structure of the sequences was predicted and compared. Phylogenetic analysis was performed by the neighbour joining tree method.
 Results: Among the selected fish species stability of acetylcholinesterase was found in fish species namely Esox lucius. The negative GRAVY score value of enzyme in all the fish species ensured better interaction and activity in the aqueous phase. It was found that the molecular weight of the acetylcholinesterase enzyme ranged between 9113 and 15991 Da. Iso-electric (pI) of acetylcholinesterase was found to be acidic in nature. GOR IV was used to predict the secondary structure of acetylcholinesterase, which showed that random coil was dominated. Neighbor joining tree of the enzyme showed that fish species named Amphiprion ocellaris as the most divergent species, while the species Oreochromis niloticus is the most primitive one.
 Conclusion: Acetlycholinesterase enzyme of Esox lucius was found to be the best compared to the other species, which possess a high number of active sites with Ile, Set and Glu rich active sites.
Highlights
Acetylcholine-mediated neurotransmission is necessary for a nervous system function
The tree is drawn to scale with branch lengths in the same unit as those of the evolutionary distances used to infer the phylogenetic tree
The study provides a better insight of the enzyme acetylcholinesterase in fishes
Summary
Acetylcholine-mediated neurotransmission is necessary for a nervous system function. Its sudden and unexpected blockade causes progressive deterioration of cognitive, autonomic and neuromuscular functions as in Alzheimer’s disease, multiple system atrophy and other conditions. In keeping with its function, AChE possesses a remarkably high specific activity, especially for a serine hydrolase functioning at a rate approaching that of a diffusion-controlled reaction [4]. The distinctive biochemical properties and physiological significance of AChE make it an interesting target for detailed structure-function analysis. Coding sequences of AChE have been cloned from a range of diverse evolutionary vertebrate and invertebrate species that include insects, nematodes, fish, reptiles, birds and several mammals, the most important among them man. The first crystal model for AChE was determined from Torpedo californica, one of the main sources of AChE for research. Crystal structures from mouse, Drosophila and man were obtained and found to be fundamentally similar
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