Modeling And Structural Analysis Of Acetylcholinesterase Enzyme Of Fishes
| dc.contributor.author | Prakasia, P. P. | en_US |
| dc.date.accessioned | 2020-09-24T08:01:50Z | |
| dc.date.available | 2020-09-24T08:01:50Z | |
| dc.date.issued | 2020-07 | |
| dc.description.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. | en_US |
| dc.identifier.affiliations | Department of Botany and Centre for Research, St. Teresa’s College (Autonomous), Ernakulam | en_US |
| dc.identifier.citation | Prakasia P. P.. Modeling And Structural Analysis Of Acetylcholinesterase Enzyme Of Fishes. International Journal of Pharmacy and Pharmaceutical Sciences. 2020 Jul; 12(7): 32-35 | en_US |
| dc.identifier.issn | 0975-1491 | |
| dc.identifier.issn | 2656-0097 | |
| dc.identifier.place | India | en_US |
| dc.identifier.uri | https://imsear.searo.who.int/handle/123456789/206122 | |
| dc.language | en | en_US |
| dc.publisher | Innovare Academic Sciences Pvt. Ltd. | en_US |
| dc.relation.issuenumber | 7 | en_US |
| dc.relation.volume | 12 | en_US |
| dc.source.uri | https://doi.org/10.22159/ijpps.2020v12i7.37762 | en_US |
| dc.subject | Acetylcholinesterase | en_US |
| dc.subject | Esox lucius | en_US |
| dc.subject | Phylogenetic analysis | en_US |
| dc.subject | CASTp | en_US |
| dc.subject | ProSA Web | en_US |
| dc.title | Modeling And Structural Analysis Of Acetylcholinesterase Enzyme Of Fishes | en_US |
| dc.type | Journal Article | en_US |
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