- ISOTOPES OF ALPHA KETOGLUTARATE AND RELATED COMPOUNDS AND THEIR USE IN HYPERPOLARIZED IMAGING
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A compound of the Formula I or a pharmaceutically acceptable salt thereof, wherein R1, Ca, Cb, Cd, and n are the same as described in the specification. Disclosed is a method of diagnosing or monitoring a patient suffering from cancer, the method comprising: administering a pharmaceutical composition comprising an effective amount of an active agent, wherein the active agent is the compound of Formula I, a pharmaceutically acceptable salt of any of the foregoing thereof, or a combination thereof, together with a pharmaceutically acceptable carrier to the patient; and diagnosing or monitoring the patient by hyperpolarized 13C-MRI. Also disclosed is a method of synthesizing 1-13C- 5-12C-diacid.
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Paragraph 0172-0175
(2021/07/24)
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- LYSINE ISOTOPOLOGUES, COMPOSITIONS COMPRISING THE SAME AND METHODS OF SYNTHESIS
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This invention relates to lysine isotopologues of Formulas I and 1-A, as described herein, and processes for synthesizing the same and derivatives and intermediates involved therein. In one aspect, described herein is a chemical compound comprising an isotopically labeled analog, i.e., an isotopologue of a standard or naturally occurring lysine. The lysine isotopologue is synthetically formed to have stable isotopes of elements incorporated at selected positions. As such, the lysine isotopologue has a molecular mass different from the mass of a standard or naturally occurring lysine.
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Paragraph 0149-0151
(2016/02/12)
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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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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.
- Beigi, Maryam,Waltzer, Simon,Fries, Alexander,Eggeling, Lothar,Sprenger, Georg A.,Müller, Michael
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supporting information
p. 452 - 455
(2013/04/10)
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- α-Hydroxy-β-keto acid rearrangement-decarboxylation: Impact on thiamine diphosphate-dependent enzymatic transformations
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The thiamine diphosphate (ThDP) dependent MenD catalyzes the reaction of α-ketoglutarate with pyruvate to selectively form 4-hydroxy-5-oxohexanoic acid 2, which seems to be inconsistent with the assumed acyl donor role of the physiological substrate α-KG. In contrast the reaction of α-ketoglutarate with acetaldehyde gives exclusively the expected 5-hydroxy-4-oxo regioisomer 1. These reactions were studied by NMR and CD spectroscopy, which revealed that with pyruvate the observed regioselectivity is due to the rearrangement-decarboxylation of the initially formed α-hydroxy-β-keto acid rather than a donor-acceptor substrate role variation. Further experiments with other ThDP-dependent enzymes, YerE, SucA, and CDH, verified that this degenerate decarboxylation can be linked to the reduced enantioselectivity of acyloins often observed in ThDP-dependent enzymatic transformations.
- Beigi, Maryam,Loschonsky, Sabrina,Lehwald, Patrizia,Brecht, Volker,Andrade, Susana L.A.,Leeper, Finian J.,Hummel, Werner,Müller, Michael
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supporting information
p. 252 - 256
(2013/02/25)
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