Please help me ask all the questions (four questions). I want the complete solution.

Q1: the following table gives the results of enzyme-catalyzed reaction. The enzyme concentration [E]=0.00012mmol/L Use the information of substrate concentration [S] and rate V0 for both experiments, with inhibitor and without inhibitor to answer the following questions 1- Calculate Km and Vmax for both experiments using Michaelis-Menten equation. [S] vs V0 2- Calculate Km and Vmax for both experiments using Lineweaver-Burk plot, 1/[S] vs 1/v0 3- Calculate Kcat for the enzyme (without inhibition) 4- Based on the values of Km and Vmax, with inhibitor and without inhibitor, determine the type of the Inhibition (competitive, non-competitive or uncompetitive) Note:- show all your work to answer the above questions. Upload your answers as one file then submit it before the due date (03-01-2024) Q1: the following table gives the results of enzyme-catalyzed reaction. The enzyme concentration [E]=0.00012mmol/L Use the information of substrate concentration [S] and rate V0 for both experiments, with inhibitor and without inhibitor to answer the following questions 1- Calculate Km and Vmax for both experiments using Michaelis-Menten equation. [S] vs V0 2- Calculate Km and Vmax for both experiments using Lineweaver-Burk plot, 1/[S] vs 1/v0 3- Calculate Kcat for the enzyme (without inhibition) 4- Based on the values of Km and Vmax, with inhibitor and without inhibitor, determine the type of the Inhibition (competitive, non-competitive or uncompetitive) Note:- show all your work to answer the above questions. Upload your answers as one file then submit it before the due date (03-01-2024)