A hypothetical enzyme that follows Michaelis-Menten kinetics functions has a substrate concentration 50mM at 50% of Vmax. Find the substrate concentration when the velocity of reaction is equal to 75% of Vmax

The process of protein decomposition by pepsin enzymes in stomach is assumed and modeled as a batch reactor. If the protein concentration over time is measured as follows:   Write the relationship between time (t), protein concentration (CA). Assuming that the enzyme reaction follows Michaelis-Menten kinetics, write the required constant (Vmax, Km), and the initial concentration of the protein is CA0.

The KM of a Michaelis-Menten enzyme for a substrate is 1.0 x 104 M. At a substrate concentration of 0.20 M, v = 43 μmol/min. Calculate the rate of reaction when the substrate concentration is tenfold lower, 0.020M. 43 μmol min rate of reaction → Vmax Км substrate concentration →

The enzymatic activity of an enzyme with Kg = 2 mM that converts substrate S into product P is measured at an initial substrate concentration S, of 10 µM. After 5 min, the substrate concentration is halved. What is the rate constant k, the maximal velocity vmax and the concentration of product after 12 min?

1) Is the ratio of the forward rate constant and reverse rate constant changed by the presence of an enzyme catalyst?   2) 4) What is the simplest mathematical relationship between substrate concentrations [S], initial velocity (Vo) of an enzyme catalyzed reaction, the maximal velocity of the reaction (Vmax), and the ½ maximal Vo (i.e. Km) ? (Hint: what is the Michaelis-Menten Equation?   3) Graphically illustrate the most useful derivation of the Michaelis-Menton equation (that darn linearized, double-reciprocal)