In silico characterization of human cytochrome P450 monooxygenases


Cytochrome P450 monooxygenases (CYPs) represent a large group and diverse family of enzymes involved in the myriad of biological processes in humans. In the present study, a total of 57 protein sequences of human CYPs retrieved from UniprotKB have been characterized for various physiochemical properties, homology search, motif and super family search and phylogenetic relationship. Physicochemical analysis showed that the isoelectric point values and GRAVY index ranged from 5.84 to 9.47 and 0.018 to -0.367, respectively. Many proteins (50 members, 87.8%) were in basic form, while few (7 members, 12.2%) were of acidic nature. Moreover, GRAVY index revealed that only CYP26C1 as hydrophobic while all others as hydrophilic. Phylogenetic analysis revealed that P450 proteins basically fall into two main clades and are divided into five subgroups. Motif analysis with MEME indicated presence, absence and even shuffling of motifs within clades. Clustering using the maximum likelihood analysis was also in accordance with P450s central roles in drug and xenobiotic metabolism as well as steroid hormone synthesis, fat-soluble vitamin metabolism, and the conversion of polyunsaturated fatty acids to biologically active molecules. Motif conservation within clusters showed the evolutionary pressure for maintenance of the structural and functional organization between different groups of protein. These results will help in the context of understanding the characteristics of the cytochrome P450 monooxygenase isoforms.

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