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

Table 4

Beta-ketoesters (BKE).

ID name	Compound name	R	(kcal/mol)	(kcal/mol)	ee (%)	Prelog	Prediction correct
BKE1	Ethyl 4-chloro-3-oxobutanoate	Chloromethyl	−46.8	−61.2	97 (S)	Anti	Y
BKE2	Ethyl 3-oxopentanoate	Ethyl	−50.2	−50.3	61 (R)	Anti	N
BKE3	Ethyl 4-methyl-3-oxopentanoate	Isopropyl	−52.0	−63.9	99 (S)	Anti	Y
BKE4	Ethyl 4,4-dimethyl-3-oxopentanoate	tert-Butyl	−47.6	−59.5	99 (S)	Prelog	Y
BKE5	Ethyl 4,4,4-trifluoro-3-oxopentanoate	Trifluoromethyl	−43.1	−58.4	90 (S)	Anti	Y
BKE6	Ethyl 3-oxo-3-phenylpropanoate	Phenyl	−54.4	−57.8	56 (S)	Prelog	Y

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 [9]. 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.