Cao_2014_J.Mol.Catal.B.Enzym_97_270

The influence of temperature and solvent on the activity of Yarrowia lipolytica Lipase 2 (YLLIP2) was investigated. This was done by interpreting experimental results with theoretical molecular modeling of the enzyme structure by using molecular dynamic (MD) simulation. The transient open conformation of YLLIP2 was obtained. It was employed for exploring the structural rearrangement of the lid and the catalytic triad (Ser162, Asp230, and His289) at different temperatures and in different solvents. The calculated results indicated that the opened extent of the lid was positively correlated with temperature and the structural rearrangement of the catalytic triad was the crucial factor for the decreased activity of YLLIP2 at higher temperature. The polar solvent molecule approaches the catalytic triad of YLLIP2 more easily and has a stronger interaction with His289 than the non-polar solvent molecule. The interaction between His289 and Asp230 was affected by the higher temperature (333 K) whereas the interaction between His289 and Ser162 was affected by the polar solvent molecule (acetone and ethanol).