Enantioselectivity and Enzyme-Substrate Docking Studies of a Ketoreductase from Sporobolomyces salmonicolor (SSCR) and Saccharomyces cerevisiae (YOL151w)
Table 3
Alpha-ketoesters (AKE).
ID name
Compound name
R1
(kcal/mol)
(kcal/mol)
ee (%)
Prelog
Prediction correct
AKE1
Ethyl 2-oxo-2-phenylacetate
Phenyl
−51.4
−51.7
99 (S)
Anti
Y
AKE2
Ethyl 2-(4-cyanophenyl)-2-oxoacetate
4-Cyanophenyl
−54.4
−64.7
82 (S)
Anti
Y
AKE3
Ethyl 2-(4-fluorophenyl)-2-oxoacetate
4-Fluorophenyl
−53.8
−39.6
74 (S)
Anti
N
AKE4
Ethyl 2-(4-chlorophenyl)-2-oxoacetate
4-Chlorophenyl
NS
−47.9
63 (S)
Anti
Y
AKE5
Ethyl 2-(4-bromophenyl)-2-oxoacetate
4-Bromophenyl
−52.2
−55.9
56 (S)
Anti
Y
AKE6
Ethyl 2-oxo-2-p-tolylacetate
4-Methylphenyl
−53.1
−55.0
88 (S)
Anti
Y
AKE7
Ethyl 2-(3,5-difluorophenyl)-2-oxoacetate
3,5-Difluorophenyl
NS
−41.7
43 (S)
Anti
Y
AKE8
Ethyl 4-methyl-2-oxopentanoate
Isopropyl
−50.2
−44.7
99 (R)
Prelog
Y
AKE9
Ethyl 4,4-dimethyl-2-oxopentanoate
tert-Butyl
−54.5
−46.4
99 (R)
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.
