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In-Silico Characterization of 14-alpha Sterol Demethylase of Aspergillus fumigatus

http://manuscript.advancejournals.org/uploads/77b66b3d7dadf55025c7f3f9b21ab46dcce908edffc964a676ec96c4c42b1668/Manuscript/8634.pdf

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 The eukaryotes sterol pathways are extremely conserved and these biosynthetic pathway are very long which includes the synthesis of dolichols, coenzyme Q, heme A, and isoprenylated proteins.14-Demethylase is an essential enzyme of the cytochrome P450 superfamily, which is potential the target of azole antifungals. Predicted results shows that 14-alpha sterol demethylase have molecular weight of 58930.8 Daltons and the theoretical isoelectric point (pI) of 7.64. The negative Grand average of hydropathicity (GRAVY)  index  of  ‐0.125. The Aliphatic index of Aspergillus fumigates 14-alpha sterol demethylase is 89.48. Alpha  helix  (Hh)  accounts   210 amino   acids   of   about   40.08%.   The   extended  strand  (Ee)  had  91  amino  acids accounting 17.37, Beta turn (Tt) made up of 51 amino acids making up 9.73% and random coil (Cc) made up of 172 amino acids accounting 32.82%. The subcellular localization of 14­alpha sterol demethylase Cyp51B was predicted to be a Plasma membrane  protein.