Lactone synthesis via biotransformations of γ-hydroxyamides

An enzyme was expressed in E. coli from a cloned amidase gene. When characterized, it was more enantioselective than commercial amidases. Three pheromones were made. An enzyme was expressed in Escherichia coli from a cloned amidase gene. When characterized, it was more enantioselective than commerci...

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Bibliographic Details
Published in:Tetrahedron: asymmetry 2004-12, Vol.15 (24), p.3819-3821
Main Authors: Taylor, Stephen K., Arnold, Carrie R., Gerds, Aaron T., Ide, Nathan D., Law, Keri M., Kling, Dale L., Pridgeon, Matthew G., Simons, Lloyd J., Vyvyan, James R., Yamaoka, Jennifer S., Liao, Min-Ken, Goyne, Thomas E.
Format: Article
Language:English
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Summary:An enzyme was expressed in E. coli from a cloned amidase gene. When characterized, it was more enantioselective than commercial amidases. Three pheromones were made. An enzyme was expressed in Escherichia coli from a cloned amidase gene. When characterized, it was more enantioselective than commercial amidases. Three pheromones were made using this biotransformation chemistry.
ISSN:0957-4166
1362-511X
DOI:10.1016/j.tetasy.2004.09.038