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  • Title: Novel mechanism of inhibition of elastase by beta-lactams is defined by two inhibitor crystal complexes.
    Author: Taylor P, Anderson V, Dowden J, Flitsch SL, Turner NJ, Loughran K, Walkinshaw MD.
    Journal: J Biol Chem; 1999 Aug 27; 274(35):24901-5. PubMed ID: 10455164.
    Abstract:
    Two structurally related beta-lactams form different covalent complexes upon reaction with porcine elastase. The high resolution x-ray structures of these two complexes provide a clear insight into the mechanism of the reaction and suggest the design of a new class of serine protease inhibitors that resist enzyme reactivation by hydrolysis of the acyl intermediate. The presence of a hydroxyethyl substituent on the beta-lactam ring provides a new reaction pathway resulting in the elimination of the hydroxyethyl group and the formation of a stabilizing conjugated double bond system. In contrast, the presence of a diethyl substituent on the beta-lactam ring leads to addition of water. The two enzyme complexes show very different binding modes in the enzyme active site.
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