Wang_2010_J.Chem.Inf.Model_50_875

T1 lipase is isolated from the palm Geobacillus zalihae strain T1 in Malaysia, functioning as a secreted protein responsible for the catalyzing hydrolysis of long-chain triglycerides into fatty acids and glycerol at high temperatures. In the current study, using 30 ns molecular dynamics simulations at different temperatures, an aqueous activation was detected for T1 lipase. This aqueous activation in T1 lipase was mainly caused by a double-flap movement mechanism. The double flaps were constituted by the hydrophobic helices 6 and 9. Helix 6 employed two major components with the hydrophilic part at the surface and the hydrophobic part inside. In the aqueous solution, the hydrophobic part could provide enough power for helix 6 to move away, driving the protein into an open configuration and exposing the catalytic triad. Our findings could provide structural evidence to support the double-flap movement, revealing the catalytic mechanism for T1 lipase.