title: TCA cycle involved enzymes SucA and Kgd, as well as MenD: efficient biocatalysts for asymmetric C-C bond formation.
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.
authors: Institute of Pharmaceutical Sciences, Albert-Ludwigs-University of Freiburg, Albertstrasse 25, 79104 Freiburg, Germany.
authors: Maryam
authors: M
authors: Beigi
authors: Simon
authors: S
authors: Waltzer
authors: Alexander
authors: A
authors: Fries
authors: Lothar
authors: L
authors: Eggeling
authors: Georg A
authors: GA
authors: Sprenger
authors: Michael
authors: M
authors: Müller
mesh_terms: D002384:Catalysis; D002952:Citric Acid Cycle / Q000235:genetics / Q000502:physiology*; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000378:metabolism; D007655:Ketoglutarate Dehydrogenase Complex / Q000378:metabolism*; D007656:Ketoglutaric Acids / Q000737:chemistry / Q000378:metabolism; D009169:Mycobacterium tuberculosis / Q000201:enzymology; D011771:Pyruvate Oxidase / Q000378:metabolism; D005680:gamma-Aminobutyric Acid / Q000031:analogs & derivatives / Q000378:metabolism
chemical_list: D029968:Escherichia coli Proteins; D007656:Ketoglutaric Acids; D005680:gamma-Aminobutyric Acid; C534108:2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase, E coli; D011771:Pyruvate Oxidase; D007655:Ketoglutarate Dehydrogenase Complex; C009338:succinic semialdehyde