Simple conformation space search protocols for the evaluation of enantioselectivity of lipases

Two computational protocols have been evaluated regarding their ability to reproduce the enthalpic part of lipase enantioselectivity by forcefield potential energy differences (Delta V-R-S(#)). Though the shortcomings of the approach are numerous, good qualitative results have been obtained here and elsewhere. The anticipated improvement of quantitative results by use of a second protocol, which did not impose any atom movement restrictions on the total system, was realized only in part. Seemingly, results depended not only on the design of the computational procedure but also on the enzyme-substrate combination modelled. With Candida antarctica lipase B, results diverged significantly more from an estimated Delta Delta H-R-S(#) than with Rhizomucor miehei lipase and cutinase.