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Inhibition of 1,4-β-d-Xylan Xylanohydrolase by the Specific Aspartic Protease Inhibitor Pepstatin
Journal of Biological Chemistry
This is the first report that describes the inhibition mechanism of xylanase from Thermomonospora sp. by pepstatin A, a specific inhibitor toward aspartic proteases. The kinetic analysis revealed competitive inhibition of xylanase by pepstatin A with an IC 50 value 3.6 ؎ 0.5 M. The progress curves were time-depended, consistent with a two-step slow tight binding inhibition. The inhibition followed a rapid equilibrium step to form a reversible enzyme-inhibitor complex (EI), which isomerizes todoi:10.1074/jbc.m407866200 pmid:15317808 fatcat:xvblurzbavgf3obxdrsqm5tx64