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- W2045734210 abstract "Valine-derived benzoxazinones have been synthesized and found to be competitive, slow-binding inhibitors of human leukocyte elastase (HLE). Steady-state inhibition constants Ki are dependent on aryl substitution and reach a maximum of potency of 0.5 nM with the 5-Cl compound 6. UV-spectral data for the interaction of HLE and the unsubstituted inhibitor 3 indicate that the stable complex formed between enzyme and inhibitor is an acyl-enzyme that can either undergo ring closure, to reform intact benzoxazinone, or hydrolysis, to liberate an N-acylanthranilic acid. Burst kinetic data, derived from the direct observation of the interaction of HLE and 3, are consistent with results of the inhibition of catalysis experiments." @default.
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- W2045734210 date "1987-06-30" @default.
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- W2045734210 title "Mechanism for slow-binding inhibition of human leukocyte elastase by valine-derived benzoxazinones" @default.
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- W2045734210 doi "https://doi.org/10.1021/bi00387a057" @default.
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