Computational Analysis of N-acetyl transferase in Tribolium castaneum

N-acetyl transferase (NAT) is responsible to catalyze the transfer of acetyl groups to arylamines from acetyl-CoA. Aralkylamine Nacetyltransferase (AANAT), which belongs to GCN5-related N-acetyl transferase member, is a globular 23-kDa cytosolic proteinthat forms a reversible regulatory complex with 14-3-3 proteins, AANAT regulates the daily cycle of melatonin biosynthesis inmammals, making it an attractive target for therapeutic control of abnormal melatonin production in mood and sleep disorders.There is no evidence available regarding α and β subunits, active site and their ASA value in Dopamine N-acetyl transferase.Therefore, we describe the development of Dopamine N-acetyl transferase model in Tribolium castaneum. We further documentthe predicted active sites in the structural model with solvent exposed ASA residues. During this study, the model was built byCPH program and validated through PROCHECK, Verify 3D, ERRAT and ProSA for reliability. The active sites were predicted inthe model with further ASA analysis of active site residues. The discussed information thus provides insight to the predicted activesite and ASA values of Dopamine N-acetyl transferase model in Tribolium castaneum.