Abstract:

Three dimensional structures of phosphotriesterase-like lactonases (PLLs) from Thermaerobacter marianensis\% were modeled by means of homology and molecular dynamics methods. On the basis of the modeling, the components and the structures of active sites TmPLLs were analyzed and compared. The docking was also performed. Arg44 was key residue for the combination of two substrates (γ-nonanoic lactone and ethyl paraoxon) with the enzyme.

Key words: phosphotriesterase-like lactonases, homology modeling, molecular docking