In silico structural, phylogenetic and drug target analysis of putrescine monooxygenase from Shewanella putrefaciens-95

Abstract

Highlights The physicochemical properties of putrescine monooxygenase from Shewanella putrefaciens-95 were compared with other known N-hydroxylating monooxygenases. The phylogenetic analysis of SpPMO and other selected class B monooxygenases clearly classified NMOs according to their substrate affinity. The molecular docking analysis of various substrates to SpPMO enzyme showed the presence of two binding pockets. Curcumin and niazirin were identified as two potential natural inhibitors to SpPMO enzyme with 2.6±0.0036 μM and 18.38±0.008 μM inhibition constants respectively.

Keywords

• N-Hydroxylating monooxygenases
• Shewanella putrefaciens
• Physicochemical characteristics
• Phylogenetic relationship
• Molecular docking
• Naturally occurring inhibitors