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

Table 5

Beta-ketonitrile (BKN).

ID name	Compound name	R	(kcal/mol)	(kcal/mol)	ee (%)	Prelog	Prediction correct
BKN1	5-Methyl-3-oxohexanenitrile	Isobutyl	−46.2	NS	99 (R)	Prelog	Y
BKN2	3-Cyclohexyl-3-oxopropanenitrile	Hexyl	NS	−38.2	99 (S)	Prelog	Y
BKN3	3-Oxo-3-phenylpropanenitrile	Phenyl	NS	−48.1	99 (S)	Prelog	Y
BKN4	3-(4-Fluorophenyl)-3-oxopropanenitrile	4-fluorophenyl	NS	−62.5	99 (S)	Prelog	Y
BKN5	3-(4-Chlorophenyl)-3-oxopropanenitrile	4-chlorophenyl	NS	−41.3	78 (S)	Prelog	Y
BKN6	3-(4-Methoxyphenyl)-3-oxopropanenitrile	4-methoxyphenyl	−43.6	NS	99 (S)	Prelog	N
BKN7	Methyl 4-(2-cyanoacetyl)benzoate	2-cyanoacetyl	NS	NS	74 (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 [7]. 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.