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. 2004 Jan;186(1):1–7. doi: 10.1128/JB.186.1.1-7.2004

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Copyright © 2004, American Society for Microbiology

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FIG. 6. — Kinetic analysis of RecA-mediated autoproteolysis of 434 repressor-DNA complexes. (A) Diagrammatic comparison of the similarities between RecA-mediated repressor autocleavage and the enzyme-catalyzed Michaelis-Menton reaction. (B) Maximum velocity of repressor autocleavage at a fixed concentration of repressor (as determined in Fig. 5) plotted as a function of the concentration of repressor-O_R1 (▪) and repressor-O_R2 (▴) complexes. The lines represent fits to the Michaelis-Menten equation. The fitting parameters are given in the text. K_D, dissociation constant; E, enzyme; S, substrate; ES, enzyme-substrate complex; P, product.