| RRC ID |
35624
|
| Author |
Patel H, Shim DJ, Farinas ET, Jordan F.
|
| Title |
Investigation of the donor and acceptor range for chiral carboligation catalyzed by the E1 component of the 2-oxoglutarate dehydrogenase complex.
|
| Journal |
J Mol Catal B Enzym
|
| 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 the Escherichia coli 2-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.
|
| Volume |
98
|
| Published |
2013-12-30
|
| DOI |
10.1016/j.molcatb.2013.09.010
|
| PMID |
24277992
|
| PMC |
PMC3837344
|
| IF |
2.269
|
| Times Cited |
1
|
| Resource |
| Prokaryotes E. coli |
JW0715
ASKA |
