title: Investigation of the donor and acceptor range for chiral carboligation catalyzed by the E1 component of the 2-oxoglutarate dehydrogenase complex.
abstract: The potential of thiamin diphosphate (ThDP)-dependent enzymes to catalyze C-C bond forming (carboligase) reactions with high enantiomeric excess has been recognized for many years. Here we report the application of the E1 component of theEscherichia coli2-oxoglutarate dehydrogenase multienzyme complex in the synthesis of chiral compounds with multiple functional groups in good yield and high enantiomeric excess, by varying both the donor substrate (different 2-oxo acids) and the acceptor substrate (glyoxylate, ethyl glyoxylate and methyl glyoxal). Major findings include the demonstration that the enzyme can accept 2-oxovalerate and 2-oxoisovalerate in addition to its natural substrate 2-oxoglutarate, and that the tested acceptors are also acceptable in the carboligation reaction, thereby very much expanding the repertory of the enzyme in chiral synthesis.
authors.affiliation: Department of Chemistry, Rutgers University, Newark, NJ 07102.
authors.forename: Hetalben
authors.initials: H
authors.lastname: Patel
authors.forename: Da Jeong
authors.initials: DJ
authors.lastname: Shim
authors.forename: Edgardo T
authors.initials: ET
authors.lastname: Farinas
authors.forename: Frank
authors.initials: F
authors.lastname: Jordan
keywords: C-C bond formation; chiral enzymatic synthesis; circular dichroism; enantioselectivity; thiamin diphosphate