Question

PLEASE JUST HELP WITH #5

In addition to competitive inhibition, there are two other common types of enzyme inhibition. One type is called uncompetitive inhibition. For this mechanism, the inhibitor can only bind to the ES complex and NOT to the free enzyme: 1. kz . E + E+P ES + 1 ESI Follow the following steps (similar, but not identical to problem 2) to derive d[P]/dt for this mechanism. (a) Write the equation for d[P]/dt (b) Write the equation for d[ESI]/dt. Apply the steady state approximation to derive an equation with (ESI) on one side and [ES], [1], and constants on the other side. (e) Write the equation for d[ES]/dt. Apply the steady state approximation and your result from part (b) to derive an equation with [ES] on one side and [E],[S], and constants on the other side (it should be a relatively simple equation). (d) For this mechanism, [E] = [E] - [ES] - [ESI). Substitute the results from parts (b) and (c) into this equation and rearrange so that [E] is on one side and everything else is on the other side. (e) Now that you have an expression for [E], you can substitute that expression back into the equation from part (b) to get [ES] in terms of measurable quantities and rate constants. (1) Take the results from part (e) and write the final expression for d[P]/dt. 5. Rearrange your final velocity equation from problem 4 into a form suitable for a Lineweaver-Burk plot. How does an uncompetitive inhibitor affect the slope of a Lineweaver-Burk plot? How does it affect the intercept? Is this what you would have expected if you had applied the same arguments that you went through in problem 1?