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• W3007341318 endingPage "1955" @default.
• W3007341318 startingPage "1949" @default.
• W3007341318 abstract "Aminotransferases are pyridoxal 5'-phosphate-dependent enzymes that catalyze reversible transamination reactions between an amino acid and an α-keto acid, playing a critical role in cellular nitrogen metabolism. It is evident that γ-aminobutyric acid aminotransferase (GABA-AT), which balances the levels of inhibitory and excitatory neurotransmitters, has emerged as a promising therapeutic target for epilepsy and cocaine addiction based on mechanism-based inactivators (MBIs). In this work, we established an integrated approach using computational simulation, organic synthesis, biochemical evaluation, and mass spectrometry to facilitate our design and mechanistic studies of MBIs, which led to the identification of a new cyclopentene-based analogue (6a), 25-times more efficient as an inactivator of GABA-AT compared to the parent compound (1R,3S,4S)-3-amino-4-fluorocyclopentane carboxylic acid (FCP, 4)." @default.
• W3007341318 created "2020-03-06" @default.
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• W3007341318 date "2020-02-18" @default.
• W3007341318 modified "2023-10-16" @default.
• W3007341318 title "Mechanism-Based Design of 3-Amino-4-Halocyclopentenecarboxylic Acids as Inactivators of GABA Aminotransferase" @default.
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• W3007341318 doi "https://doi.org/10.1021/acsmedchemlett.9b00672" @default.
• W3007341318 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7549257" @default.
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