Molecular Design of Thermostable Alcohol Dehydroganase for Synthesis for Chiral Aromatic Alcohols
Chiral aromatic alcohols are important building blocks for a variety of high-value chemicals, including pharmaceuticals, agrochemicals, and various other chiral compounds. Generally only one enantiomer is biologically active for the intended purpose of the drug; the other enantiomer can be toxic. To achieve enantiomeric purity using current methods of traditional chemical synthesis, a reaction must either be fed a chiral feedstock or comprise an additional separation step, either of which can be time consuming and/or very costly. Therefore, there is a need for more efficient ways of producing stereomerically pure compounds.
Description of Technology
Michigan State University’s invention involves compositions and methods utilizing thermostable and novel alcohol dehydrogenase enzymes for biosynthesizing chrial specific molecules for use as precurson molecules in synthesizing pharmaceutical compounds. It describes the design of novel, heat stable enzymes that can be used to produce stereomerically pure compounds (more pure drugs), reducing the need for additional, costly, purification steps.
- The technology is a good template to engineer an industrially attractive catalyst for chiral chemical synthesis.
- The need for a generation of stereo-specific molecules exists.
The invention is useful in drug precurson synthesis and more cost effective methods for producing some pharmaceuticals and agrochemicals.
U.S. patent 7,750,135
J. Gregory Zeikus, Karla Fjeld, Claire Vieille
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Michigan State University