Molecular dynamics simulation and functional motions study of Bacillus subtilis lipase A

Bacillus subtilis lipase A is the smallest member of α/β hydrolase family with no interfacial activation property. Bacillus subtilis lipase A has numerous applications as well as other lipases، such as industrial، pharmaceuticals، environmental and food products. There have been presented several reports about the engineering of this enzyme based on the random mutagenesis. Therefore، study of molecular dynamics simulation of the enzyme at different temperatures seems to be necessary to understand its dynamical properties. Understanding of such molecular motions is important to switch from random to rational design of the enzyme. Two flexible loops have been identified based on 15 ns molecular dynamics simulation of the enzyme. The extent of flexibility for the loops was different at three temperatures. On the other hand، two critical loops have been identified to play important role on the functional motions of the enzyme as hinges of the axial motions of the secondary elements around the active site cleft.