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

Table 7

Beta-ketoesters (BKE).

ID name	Compound name	R	(kcal/mol)	(kcal/mol)	ee (%)	Prelog	Prediction correct
BKE1	Ethyl 4-chloro-3-oxobutanoate	Chloromethyl	−46.3	−34.8	98 (R)	Prelog	Y
BKE2	Ethyl 3-oxopentanoate	Ethyl	−55.3	−47.3	98 (S)	Prelog	N
BKE7	Ethyl 3-oxobutanoate	Methyl	−51.2	−52.0	98 (S)	Prelog	Y
BKE8	Ethyl 3-oxohexanoate	n-Propyl	−56.5	−47.9	98 (S)	Prelog	N

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.