1. Glycolysis

2. Transition step

3. TCA cycle

4. Electron transport chain

For each of the above, answer the following questions:

Where in the cell does it take place? Prokaryote vs Eukaryote

Number of ATP molecules produced?

Number of NADH/FADH2 produced?

What goes in, and what leaves? (reactants vs end products)

Substrate-level phosphorylation to yield ATP occurs during which stage(s) of aerobic respiration?

The standard free energy change of phosphate hydrolysis is shown below for several molecules in the glycolytic pathway.

Which statement explains why glucose phosphorylation could not occur without ATP investment?
A.   Without ATP investment in stage I of glycolysis, the concentration of ATP would become too high and would inhibit phosphofructokinase, leading to inhibition of the entire glycolytic pathway.

B.   Without ATP investment, glucose would not become "trapped" in the cell and could easily be transported out as blood glucose levels decrease. This transport would reduce the amount of glucose available for some organs.

C.   Without ATP investment it would be impossible to regulate the entry of glucose into glycolysis.

D.   Without ATP investment, one or both of the substrates would need to exceed the solvent capacity of the cell for glucose phosphorylation to occur.

What are the physical and chemical properties of enzyme active sites. Use the enolase mechanism to illustrate as many of these as you can.

Can ACE (Angiotensin-converting enzyme)  inhibitiors and angiotensin receptor blockers be used in hypertensive patients with renal insufficiency?

How do the two enzymes, phosphorylase kinase and phosphoprotein phosphatase, work together to regulate the glycogen phosphorylase enzyme?

If de novo fatty acid synthesis is active would you expect malic enzyme to be active or not? Please explain.

in Hereditary hyperammonemia:

- Define it

- In a table write the types of hyperammonemia & its defective enzyme

- Write about the drug treatment of it

An enzyme catalyzed reaction has a Km of 3.76 mM and a Vmax of 6.72 nM/s. What is the reaction velocity in nM/s, when the substrate concentrations are:

A. 0.500 mM

B. 15.6 mM

C. 252 mM

D. Now assume you have added a competitive inhibitor that has a concentration of 15.6 µM with a K_I of 7.30 µM to the enzyme in question 9. Calculate the velocity at the same substrate concentrations as above:

E. 0.500 mM

F. 15.6 mM

G. 252 mM