Two haloalkane dehalogenases were tested for their ability to perform kinet
ic resolutions of a series of racemic substrates and to convert meso substr
ates enantioselectively. For the kinetic resolutions E-values of up to 9 we
re measured and, in the conversions of the meso substrates, products were o
btained with an enantiomeric excess of up to 47%. A kinetic analysis reveal
ed that despite modest overall chiral recognition (expressed as E-values),
there are large differences between the K-m values (>100 fold) of two enant
iomeric substrates but that these differences are compensated by correspond
ingly large differences in k(cat). (C) 2001 Elsevier Science Ltd. All right
s reserved.