Figure 2 | Scientific Reports

Figure 2

From: Variance-corrected Michaelis-Menten equation predicts transient rates of single-enzyme reactions and response times in bacterial gene-regulation

Figure 2

Similarities and differences in enzyme kinetics and transcriptional gene-regulation.

(A) In an enzymatic reaction, substrate S and enzyme E form a complex SE, which turns into a complex PE of product and enzyme. The product P is released in the final step. As a consequence, the number of substrate-molecules in the reservoir is decreased by one. (B) In transcriptional gene-regulation, a TF molecule first binds the DNA non-specifically and finds its specific binding site, the operator O, by sliding along the DNA. The operator bound TF changes the DNA conformation or interacts with RNA polymerase (RNAP) directly, which changes the transcription rate of the target gene. The TF molecule is returned to the reservoir of free TF upon unbinding from the DNA and therefore the total number of TF is conserved. The probability of the complex states (third step) both in enzyme kinetics and gene-regulation is described by a Michaelis-Menten type equation as discussed in the main text.

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