6 research outputs found

    MALDI-TOF MS/MS analysis of the hNAAA tryptic peptide T10-β after covalent modification.

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    <p>Tandem MALDI-TOF MS/MS spectra of the T10-β peptide (sequence: CTSIVAQDSR) demonstrates covalent modification of Cys126 by both AM6701 (Panel (A)) and <i>N-</i>Cbz-serine β-lactone (Panel (B)).</p

    Representation of the active site of hNAAA after treatment with <i>N-</i>Cbz-serine β-lactone.

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    <p>Homology model illustrates acylated catalytic nucleophile Cys126 after treatment with <i>N-</i>Cbz-serine β-lactone.</p

    Potencies of hNAAA inhibitors.

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    <p>The <i>k</i><sub>inact</sub> and <i>K</i><sub>I</sub> values for the covalent inhibitors were obtained as described in the Experimental Procedures. The IC<sub>50</sub> values were calculated after 2 hours preincubation of the enzyme and inhibitor before addition of the substrate. Values are averages ± SD of three independent experiments.</p

    Representation of the active site of hNAAA after treatment with AM6701.

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    <p>Homology model illustrates thiocarbamylation of catalytic nucleophile Cys126 after treatment with AM6701.</p

    Concentration dependent inhibition of purified hNAAA by three compounds.

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    <p>hNAAA was incubated with the compounds AM6701 (squares), <i>N-</i>Cbz-serine β-lactone (circles), and AM9023 (diamonds) for two hours in order to reach full inhibition before measuring activity. Panel (A). A radioactivity-based assay with [<sup>14</sup>C] PEA as substrate. Panel (B). A fluorescence-based assay with PAMCA as substrate. Representative curves are displayed.</p
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