The a/�-hydrolase super family of enzymes includes a wide variety of enzymes, such ascarboxylesterases, lipases, cholinesterases, epoxide hydrolases, and haloalkane dehydrogenases.Serine hydrolase enzymes are a subfamily of the a/�-hydrolase super family and are known fortheir ability to catalyze the hydrolysis of various ester, amide, and thioester moieties of variousendogenous and exogenous compounds. To better understand structure-function relationshipswithin the serine-hydrolase family of enzymes, insight into their dynamical properties, inparticular their low-frequency motions and thermal stabilities, is required. Here we presentresults for three model enzymes from the a/�-hydrolase family in our study: pnbCE, which is abacterial carboxylesterase; cutinase, which is a fungal esterase enzyme; and thermusthermophilus HB8, which is a hypothetical protein lacking the catalytic residues. Long-timedynamics, temperature - dependent structural properties, and thermal stabilities associated withthese enzymes are studied using molecular dynamics simulations and normal mode analysis withan all atom force field (ff99SB).Normal modes analysis data reveal a collective, low frequency motion in these enzymes,which is a scissor-like motion of the two large loops surrounding the entrance to the active site,in case of pnbCE and cutinase enzymes. By analyzing this particular mode of motion in HB8enzyme, after its structure has been aligned with other two enzyme systems, we have predictedlocation of the possible active site for the HB8 enzyme.Results and insights from our computational work will be presented in this poster.

Insights into the long-time dynamics, structural properties, and thermalstabilities of serine hydrolase enzymes from molecular dynamics and normal mode analysis

245th National Meeting (2013)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.