The importance of helical structures to the overall activity and structural stability of a lipase from Pseudomonas aeruginosa PAO1 in n-hexane.

Bacterial lipases are versatile extracellular enzymes with a catalytic triad at the active site and a flexible 'lid' that modulates catalytic accessibility. We combined computational modeling with preliminary in vitro testing to assess the structural stability and activity of the Pseudomonas aeruginosa PAO1 lipase (PAL). We evaluated several systems consisting of the native and mutant forms of the lipase in n-hexane using molecular dynamics simulations.