Functional and physiochemical characterization of a hypothetical protein of Cytochrome p450 in fungi

Abstract

Cytochrome P450 belongs to membrane-bound hemoprotein generally present in the all domains system such as animals, plants, fungi, protists, bacteria, and archaea. They play most fascinating roles as bio-catalysis in different chemical reactions like bio-remediation, bio-degradation, detoxification, bio-conversions as well as in metabolism of drugs. Current study has focused on structure and function analysis of CYP in Fusarium oxysporum through computation tools. The structural analysis showed that it contained more hydrophobic amino acids and highest 45.26% of α-helix while the functional analysis showed that intracellular and topology of both alpha-helical and beta-barrel transmembrane CYP protein is globular nature. Procheck analysis shows that ramachandran favored regions are 95.09%.  Evolutionary aspect studied with clustal omega, F. oxysporum CYP 51 is more similar to A. alliaceus because both of species share same ancestor. The protein-protein interactions investigation showed that F. oxysporum CYP shows closely relations with squalene synthase and terpene cyclase.