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- Title
In-Silico CHARACTERIZATION OF 14-ALPHA STEROL DEMETHYLASE OF Aspergillus fumigatus.
- Authors
Verma, Pravesh; Yadav, Navneet Kumar; Sarvendra, Kunwar; Srivastava, A. K.
- Abstract
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.
- Subjects
STEROLS; DEMETHYLASE; ASPERGILLUS fumigatus
- Publication
Journal of Recent Advances in Applied Sciences, 2015, Vol 29, Issue 1, p1
- ISSN
0970-1990
- Publication type
Article