Stereoselective catalysis controlled by a native leucine or variant isoleucine wing‐gatekeeper in 2‐haloacid dehalogenase

Comprehensively understanding enzymatic stereoselectivity will assist in the creation of new enzymes for producing optically pure compounds for chemical applications. The essential features for selecting enantiomers are controlled by particular residues or regions of the enzymes. We report a stereoselective mechanism in the D‐2‐haloacid dehalogenase HadD AJ 1, in which L288 is identified as a gatekeeper in the access channel that strictly...