Research Article

Enantioselectivity and Enzyme-Substrate Docking Studies of a Ketoreductase from Sporobolomyces salmonicolor (SSCR) and Saccharomyces cerevisiae (YOL151w)

Table 6

Alpha-ketoesters (AKE).

124289.table.006

ID nameCompound nameR (kcal/mol) (kcal/mol)ee (%)PrelogPrediction correct

AKE10Ethyl 2-oxobutanoateEthyl−54.4−42.352 (S)PrelogN
AKE11Ethyl 2-oxopentanoaten-Propyl−46.5−46.298 (R)AntiY
AKE12Ethyl 2-oxo-4-phenylbutanoatePhCH2CH2NS−56.398 (S)AntiY

NS = no structure found meeting the requirements. and refer to the lowest energy docking pose that meets the criteria for valid structure whose geometry is pro or , respectively. Literature values for the enantiomeric excess (ee (%)) were obtained from [26]. Prelog column indicates if the enzyme followed prelog or antiprelog rule for the given substrate. The last column indicates if the model correctly predicted the experimental results.