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TCA cycle involved enzymes SucA and Kgd, as well as MenD: efficient biocatalysts for asymmetric C-C bond formation.
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- Additional Information
- Source:
Publisher: American Chemical Society Country of Publication: United States NLM ID: 100890393 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1523-7052 (Electronic) Linking ISSN: 15237052 NLM ISO Abbreviation: Org Lett Subsets: MEDLINE
- Publication Information:
Original Publication: Washington, DC : American Chemical Society, c1999-
- Subject Terms:
- Abstract:
Asymmetric mixed carboligation reactions of α-ketoglutarate with different aldehydes were explored with the thiamine diphosphate dependent enzymes SucA from E. coli, Kgd from Mycobacterium tuberculosis, and MenD from E. coli. All three enzymes proved to be efficient biocatalysts to selectively deliver chiral δ-hydroxy-γ-keto acids with moderate to excellent stereoselectivity. The high regioselectivity is due to the preserved role of α-ketoglutarate as acyl donor for these enzyme-catalyzed reactions.
- Accession Number:
0 (Escherichia coli Proteins)
0 (Ketoglutaric Acids)
56-12-2 (gamma-Aminobutyric Acid)
EC 1.2.3.3 (2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase, E coli)
EC 1.2.3.3 (Pyruvate Oxidase)
EC 1.2.4.2 (Ketoglutarate Dehydrogenase Complex)
M73BX3CPMU (succinic semialdehyde)
- Publication Date:
Date Created: 20130116 Date Completed: 20130610 Latest Revision: 20181202
- Publication Date:
20221213
- Accession Number:
10.1021/ol3031186
- Accession Number:
23317369
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