Research Article

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

Table 2

Aliphatic ketones (ApK).

124289.table.002

ID nameCompound nameR1R2 (kcal/mol) (kcal/mol)ee (%)PrelogPrediction correct

ApK1Heptan-2-onen-PentylCH3−43.3−41.230 (S)PrelogN
ApK2Octan-2-onen-HexylCH3−46.8NS44 (S)PrelogN
ApK3Nonan-2-onen-HeptylCH3−47.3NS4 (R)AntiY
ApK41-Adamatyl methyl ketone1-AdamantylCH3−45.1−46.9>99 (S)PrelogY
ApK5Octane-3-onen-PentylCH2CH3−45.1−42.572 (R)PrelogY

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.