Gthe results of kinetic experiments of an unidentified enzyme were used to create a plot of the initial reaction velocity ) versus the substrate concentration ([s]). a plot of the initial reaction velocity versus substrate concentration shows four data points connected by a curve. the x-axis plots the substrate concentration and is scaled from zero to 450 nanomolar. the y-axis plots the initial reaction velocity and is scaled from zero to 0.35 micromoles per minute. the slope of the curve is steep initially but becomes shallower as the substrate concentration increases. the enzyme kinetics data were also used to create a double‑reciprocal plot of versus 1[s]. a double-reciprocal plot of one over the initial reaction velocity versus 1 over the substrate concentration shows four data points connected by a trend line. the x-axis plots the inverse of the substrate concentration and is scaled from negative 0.01 to positive 0.025. the y-axis plots the inverse of the reaction velocity and is scaled from negative 2 to positive 12. the linear trend line has a positive slope with a y-intercept of positive 2 and an x-intercept of negative 0.005. does it appear that the enzyme follows michaelis–menten kinetics?