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• W2019186845 abstract "The synthesis of a new inhibitor, N-phosphonacetyl-l-isoasparagine (PALI), of Escherichia coli aspartate transcarbamoylase (ATCase) is reported, as well as structural studies of the enzyme·PALI complex. PALI was synthesized in 7 steps from β-benzyl l-aspartate. The KD of PALI was 2 μM. Kinetics and small-angle X-ray scattering experiments showed that PALI can induce the cooperative transition of ATCase from the T to the R state. The X-ray structure of the enzyme·PALI complex showed 22 hydrogen-bonding interactions between the enzyme and PALI. The kinetic characterization and crystal structure of the ATCase·PALI complex also provides detailed information regarding the importance of the α-carboxylate for the binding of the substrate aspartate." @default.
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• W2019186845 date "2006-09-02" @default.
• W2019186845 modified "2023-10-16" @default.
• W2019186845 title "<i>N</i>-Phosphonacetyl-<scp>l</scp>-isoasparagine a Potent and Specific Inhibitor of <i>Escherichia </i><i>c</i><i>oli</i> Aspartate Transcarbamoylase" @default.
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• W2019186845 doi "https://doi.org/10.1021/jm0607294" @default.
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