Chemoenzymatic synthesis of glutamic acid analogues: substrate specificity and synthetic applications of branched chain aminotransferase from Escherichia coli.
J Org Chem
; 72(20): 7560-6, 2007 Sep 28.
Article
en En
| MEDLINE
| ID: mdl-17718503
A new route to alpha-keto acids is described, based on the ozonolysis of enol acetates obtained from alpha-substituted beta-keto esters. Escherichia coli branched chain aminotransferase (BCAT) activity toward a variety of substituted 2-oxoglutaric acids was demonstrated analytically. BCAT was shown to have a broad substrate spectrum, complementary to that of aspartate aminotransferase, and to offer access to a variety of glutamic acid analogues. The usefulness of BCAT was demonstrated through the synthesis of several 3- and 4-substituted derivatives.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Ácido Glutámico
/
Escherichia coli
/
Transaminasas
/
Ácidos Cetoglutáricos
Idioma:
En
Revista:
J Org Chem
Año:
2007
Tipo del documento:
Article
País de afiliación:
Francia
Pais de publicación:
Estados Unidos