Identification of novel cytochrome P450 homologs using overlapped conserved residues based approach

Abstract

Cytochrome P450 enzymes are one of the most versatile biological catalysts that are found in nature. They have potentials as a drug target in pharmaceutical industries, as a biocatalyst in bioconversion process in chemical industries, and as a biosensor in biomedical industries. Proteins in CYPs superfamily are closely related in structural and functional properties but share low sequence similarity, which makes the identification and characterization of the novel P450 homologs a challenging task. In this study, the overlapped conserved residue (OCR) based approach was used to identify the fingerprints for the alpha-helical rich CYPs, and they were tested to detect novel P450 homologs in the NCBI non-redundant protein sequence database. We could identify 13 potential novel P450 sequence homologs, which were validated at the sequence and structural levels for the presence of the conserved PROSITE motif and conserved Cytochrome P450 structure domain, respectively. This study suggests that the OCR-based approach can be a useful way to detect novel homologous a-helix rich proteins such as Cytochrome P450s.