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

<table>Mechanism of stereoselectivity for NAD(P)H-dependent ketoreductase (1Y1P) and homology model of YOL151w. Group priorities are based on Cahn-Ingold-Prelog rules and assumed in the schemeto be OH &gt; R<sub>1</sub> &gt; R<sub>2</sub>. B represents any residue capable of donating a hydrogen atom.</table>

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Scheme 1

Scheme 1: Enantioselectivity and Enzyme-Substrate Docking Studies of a Ketoreductase from <i>Sporobolomyces salmonicolor</i> (SSCR) and <i>Saccharomyces cerevisiae</i> (YOL151w) 

Scheme 1 | Enantioselectivity and Enzyme-Substrate Docking Studies of a Ketoreductase from Sporobolomyces salmonicolor (SSCR) and Saccharomyces cerevisiae (YOL151w) 