title: Molecular-modeling calculations of enzymatic enantioselectivity taking hydration into account.
abstract: A new molecular-modeling methodology has been applied to explain enzymatic enantioselectivity in water. This methodology, which combines vacuum molecular mechanics and the continuum solvation method, should provide a more realistic view of the solvent-enzyme and solvent-substrate interactions than the heretofore used approaches involving the vacuum molecular mechanics only. The methodology described herein has been validated using the experimental data on alpha-chymotrypsin's enantioselectivity in the hydrolysis of four chiral substrates. The reasons why the vacuum molecular mechanics, although not taking hydration into account, still in most cases provide a satisfactory approximation of reality are discussed.
authors: Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
authors: T
authors: T
authors: Ke
authors: B
authors: B
authors: Tidor
authors: A M
authors: AM
authors: Klibanov
mesh_terms: D002918:Chymotrypsin / Q000737:chemistry / Q000378:metabolism; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D011487:Protein Conformation; D013237:Stereoisomerism; D014618:Vacuum; D014867:Water
chemical_list: D004798:Enzymes; D014867:Water; D002918:Chymotrypsin