You are working on an enzyme that obeys standard Michaelis-Menten kinetics. You have determined the Vmax to be 0.1 mol/sec and the K to be 2.5 mM. What would the rate of the reaction be when the substrate concentration is 20 mM? Ⓒ 0.09 Ms¹ O 0.133 MS-1 O 0.18 Ms¹¹ 09 MS-¹ O 0.018 Ms¹ O 0.2 MS-¹

You begin to study enzyme Z, which catalyzes a simple reversible reaction that interconverts compound S and compound P. You observe that the ∆G´° for the S to P conversion to be –6 kJ/mol, and that compound S has ∆G´° for binding to enzyme Z of –15 kJ/mol, while compound P has a ∆G´° for binding to enzyme Z of –13 kJ/mol. Please explain the effect of enzyme Z on conversion of S to P. (Your answer should include a graph qualitatively  showing energy versus reaction progress; however, you still need to explain youranswer in words!) not sure how to make the correct graph.

When reviewing a Michaelis-Menten Saturation Curve, at first the rate of the reaction is relatively constant, but the rate decreases as the substrate is used up and eventually reaches a plateau. Afte reaching this plateau, what would speed up the reaction again? Adding more substrate Adding heat Adding more enzyme Adding cofactors

For an enzyme-catalyzed reaction, the velocity was determined at two different concentrations of the substrate. Estimate the value of Vmax. [S] (MM) 10 20 88 nmol/min 79 nmol/min 67 nmol/min V(nmol/min) 51 nmol/min 27 Not enough information is given to form a reasonable estimation. 48