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Molecular docking analysis of Omt-A protein model from Aspergillus flavus with synthetic compounds

Aflatoxin is a potent mycotoxin of Aspergillus flavus that has been classified as a Group I carcinogen. O-methyltransferase A (Omt-A) is a critical enzyme in the formation of aflatoxin. It catalyzes the methylation of norsalic acid to form the highly toxic intermediate averantin. The ligand-protein...

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Detalles Bibliográficos
Autores principales: Kumar, Maneesh, Sahoo, Ganesh Chandra, Ansari, Waquar Akhter, Mohammad, Ajmal Ali, Mohammad, Abul Farah, Lee, Joongku
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Biomedical Informatics 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10640793/
https://www.ncbi.nlm.nih.gov/pubmed/37969662
http://dx.doi.org/10.6026/97320630019990
Descripción
Sumario:Aflatoxin is a potent mycotoxin of Aspergillus flavus that has been classified as a Group I carcinogen. O-methyltransferase A (Omt-A) is a critical enzyme in the formation of aflatoxin. It catalyzes the methylation of norsalic acid to form the highly toxic intermediate averantin. The ligand-protein interaction of Omt-A was performed with piperlonguminin and blasticidins. The maximum affinity of -10.6 was found for the 5ICC_A piperlonguminine at site1 (X,Y,Z: -15.282, 21.785, 5.672). Compounds such as Blasticidin S, Neoeriocitrin, Blasticidin S - hydrochloric acid, 6,6''-Bigenkwanin, Pipernomaline, and Eriodictyol were found to have binding features to protein residues, as shown by computational interaction at the molecular level.