Investigation of the donor and acceptor range for chiral carboligation catalyzed by the E1 component of the 2-oxoglutarate dehydrogenase complex

Hetalben Patel, Da Jeong Shim, Edgardo T. Farinas, Frank Jordan

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

The potential of thiamin diphosphate (ThDP)-dependent enzymes to catalyze CC 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.

Original languageEnglish (US)
Pages (from-to)42-45
Number of pages4
JournalJournal of Molecular Catalysis B: Enzymatic
Volume98
DOIs
StatePublished - 2013

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Bioengineering
  • Biochemistry
  • Process Chemistry and Technology

Keywords

  • CC bond formation
  • Chiral enzymatic synthesis
  • Circular dichroism
  • Enantioselectivity
  • Thiamin diphosphate

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