Biocatalytic Routes to Statin Side Chains

The Development of Short, Efficient, Economic, and Sustainable Chemoenzymatic Processes 

A wild-type DERA with less than 30% sequence identity to the E. coli enzyme led to a significant improvement over the E. coli wild-type DERA-based process originally described by Wong [15], The application of rational mutagenesis, based on the available crystal structure of the E. coli enzyme, expanded the range of suitable acceptor substrates for DERA to azido-substituted aldehydes, further facilitating access to, for example, the atorvastatin side chain [16]. 

2-Deoxy-D-Ribose 5-Phosphate Aldolase (DERA)-Based Routes to 

The beauty and the economic advantage of the DERA-based processes to certain statin side chains is based on the fact that the carbon skeleton and the two chiral centers of the side chains are built up in one step from the simple, cheap starting materials acetaldehyde and chloroacetaldehyde. This compensates for the higher biocatalyst loading required by the DERA approach compared with the other bio-catalytic processes summarized above, as will be described in the following sections. 

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