The whole cells of Candida parapsilosis ATCC 7330 are a well-established biocatalyst used for oxidation and reduction of various organic compounds to generate chiral synthons. Recombinantly expressed carbonyl reductase (CpCR) from the same strain reduces aryl α–ketoesters to their respective optically pure alcohols but preferentially reduces aliphatic and aryl aldehydes to primary alcohols. The prochiral substrates viz. aryl α-ketoester [Ethyl-2-oxo-4-phenylbutanoate], aryl ketone [Acetophenone] and aliphatic β-ketoester [Ethyl-4,4,4-trifloro-3-oxo-butanoate] get reduced to (R)-alcohols with CpCR while an aryl ketoaldehyde [2-oxo-2-phenylacetaldehyde] gives the (S)-alcohol. The optimal orientation required for the high conversion and desired enantioselectivity was analyzed by docking the α/β ketoesters, ketoaldehyde and a ketone with a modeled CpCR. Aryl α-ketoester, having the lowest free energy (-8.43 kcal/mol), shows the most favorable binding with CpCR (Interaction Energy = 7.9 kcal/mol). Also, the close proximity of aryl α-ketoester to the cofactor NADPH (2.82 Å) facilitates a better Pro-R hydride transfer as compared to other substrates. © 2018 Elsevier B.V.