PLEASE HELP The following data were obtained from the double-reciprocal plot of a single-substrate enzyme that obeys Michaelis-Menten kinetics, i. e., that gives a hyperbolic substrate saturation curve:

Kinetic Constants Without inhibitor
Vmax (micromol/min):50
Km (micromoles/liter):10

With inhibitor X (100 microM)
Vmax (micromol/min):50
Km (micromoles/liter):25

Ten micrograms of enzyme were used in the activity assay, which had a total volume of 2 ml. The molecular weight of the enzyme, which functions as a monomer, is 50,000 Daltons (g/mol). (a) What kind of inhibitor is X? (b) Calculate the dissociation constant for X from its complex with enzyme E (c) Calculate the catalytic rate constant for the enzyme (d).calculate the initial velocity of the enzyme-catalyzed reaction at a substrate concentration of 20 microM (1) in the absence of any inhibitor and (2) in the presence of 100 microM inhibitor X. (e) Calculate the fraction of the enzyme that has substrate bound (1) in the absence of inhibitor and (2) in the presence of inhibitor at the concentration indicated. (f) State whether or not your answer makes sense in terms of what type of inhibitor X is. Explain