Computational studies of cytochrome P450 (CYPs) enzyme in pulses
Abstract
Cytochrome P450 (CYP450) is a large superfamily of enzymes found in all domains of life, including
plants. It plays a crucial role in the metabolism of various compounds, including drugs, toxins, and
endogenous substrates. Pulses are the richest source of fiber and complex carbohydrates, resulting in a
low GI food. CYP450s enzymes are heme-containing monooxygenases that catalyze metabolisms of
various endogenous and exogenous compounds. They constitute a superfamily of enzymes present in
various organisms including mammals, plants, bacteria, and insects. CYP450s are diverse and
metabolize a wide variety of substrates, but their structures are largely conserved. In this study,
bioinformatics analyses of CYP450s enzyme performed in pulses. According to the conserved motifs
obtained by MEME and MAST tools, ten motifs were common in all those pulses. The structural and
functional analyses of CYP450s in pulses were done by using UniProtKB and InterProScan tools in
ExPASy database. The tertiary structures of pulses were predicted by Phyre2 web server. The protein
sequences were aligned with ClustalW and then the phylogenetic tree was constructed by MEGA11
using the neighbor-joining (NJ) method. By the successful analysis of CYP450s, we developed a
productive database by using MYSQL and PHP. The database provides information related to 200
proteins of P450s in pulses with their predicted 3D structure in PDB format, functions and Fasta
sequences. A Pulses Cytochrome P450 database serves as a centralized repository for curated
information on CYP450 enzymes in pulses. It consolidates data from various sources, including
sequence information, structural data, substrate specificity, and catalytic properties.