Fig. 3: Substrate-inhibition kinetics of StvP2 catalyzing MDB formation. | Nature Communications

Fig. 3: Substrate-inhibition kinetics of StvP2 catalyzing MDB formation.

From: Uncovering the cytochrome P450-catalyzed methylenedioxy bridge formation in streptovaricins biosynthesis

Fig. 3

a Calibration curve of 3 by HPLC-DAD with the peak area (A) as a function of substrate concentration (C) for quantification. b Kinetic curves of StvP2 converting 2, 4, and 6 to form 1, 3, and 5, respectively, fitted with modified Hill model by Origin. Initial velocities were expressed with product formation relative to 1 μM enzyme. All the enzymatic kinetic experiments are conducted independently in triplicate (n = 3), and all the independent data points are plotted with red diamonds, yellow circles, and blue triangles respectively in b. Source data are provided as a Source data file.

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