Biocatalytic strategy toward asymmetric β-hydroxy nitriles and γ-amino alcohols

A library of 20 bakers’ yeast reductases, that are overexpressed in Escherichia coli, were screened against a variety of β-keto nitriles. Enzymes from the aldose reductase and the short chain dehydrogenase family displayed activity toward these substrates. All of the seven substrates were reduced wi...

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Bibliographic Details
Published in:Tetrahedron letters 2011-05, Vol.52 (19), p.2440-2442
Main Authors: Nowill, Randall W., Patel, Trisha J., Beasley, David L., Alvarez, Jose A., Jackson, Elizah, Hizer, Todd J., Ghiviriga, Ion, Mateer, Scott C., Feske, Brent D.
Format: Article
Language:English
Subjects:
Alcohols
Aliphatic compounds
Asymmetry
Bakers’ yeast
Biocatalysis
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
Chains
Chemistry
Drugs
Enzymes
Exact sciences and technology
Fundamental and applied biological sciences. Psychology
Inhibitors
Methods. Procedures. Technologies
Nitriles
Organic chemistry
Preparations and properties
Reductase
Reductases
β-Keto nitrile
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Summary:A library of 20 bakers’ yeast reductases, that are overexpressed in Escherichia coli, were screened against a variety of β-keto nitriles. Enzymes from the aldose reductase and the short chain dehydrogenase family displayed activity toward these substrates. All of the seven substrates were reduced with high enantioselectivities and in some cases both antipodes could be synthesized in high ees. These whole-cell reactions afforded gram quantities of asymmetric compounds that could ultimately lead to scaleable and simple synthesis to new drug analogs of serotonin reuptake inhibitors and β-adrenergic blocking agents.
ISSN:0040-4039
1873-3581
DOI:10.1016/j.tetlet.2011.03.009