In silico analysis of chloroperoxidase and lignin peroxidase of pathogenic fungus macrophomina phaseolina

Macrophomina phaseolina is a destructive fungus that affects more than 500 plant species throughout the world. Lignin degradation of the host plant is crucial step for the pathogenesis of this fungus. Chloroperoxidase and lignin peroxidase are two important enzymes for lignin degradation. To develop an effective antagonist against this fungus, understanding these proteins is necessary. In this study, we have reported physico-chemical characteristics, phylogenic relationship, secondary structure, 3-D structure, motifs of 7 chloroperoxidase and 3 lignin peroxidase proteins. Moreover, pockets as well as conserved residues in the motif sequence were identified as the target for site-directed mutagenesis of chloroperoxidase and lignin peroxidase. This mutagenesis or designing target ligands against these proteins may stop the ligninolytic activity of M. phaseolina, which would save economically important plants.