Abstract
Cytochrome P450 monooxygenase isolated from anti-malarial Artemisia annua L. plants belongs to the family Asteraceae is involved in artemisinin biosynthesis considered as a vigorous anti-malarial drug. To understand the structural and functional features of amorpha-4,11-dienemonooxygenase, a variant of cytochrome P450 monooxygenase (CYP71) may help in the up-regulation of artemisinin. In this context, biocomputational approaches were used to study the amorpha-4,11-diene monooxygenase catalytic features related to other biosynthetic enzymes targeted from artemisinin biosynthesis. The full-length gene was cloned from a high yielding artemisinin strain of the A. annua L. plant with size of (2054 bp) and encodes for the CYP71 protein (495aa) protein residues with different conserved domains/motifs. The molecular weight similar to 55.73kDa and isoelectric point 9.13 of CYP were observed through in silico analysis. The phylogenetic analysis revealed that cyp71 gene of A. annua was evolutionary conserved with other plant species of cytochrome family. The Modelled 3D structure of CYP71 protein has shown the catalytic relationship between the three different ligand molecules such as farnesyl pyrophosphate (FPP), omega 4,11-diene (AD) and artemisinic alcohol (AA). The in silico information showed a key role of binding of these molecules for up-regulation of artemisinin biosynthesis and its accumulation.