18. A transition-state analog:
a. is less stable when binding to an enzyme than the normal substrate.
b. resembles the active site of general acid-base enzymes.
c. resembles the transition-state structure of the normal enzyme-substrate complex
d. stabilizes the transition state for the normal enzyme-substrate complex.
e. typically reacts more rapidly with an enzyme than the normal substrate.

12. Antibodies are used for the following purposes (circle all that apply):
a. to specifically labeling proteins in electrophoresis assays
b. as catalysts
c. as FDA-approved drugs
d. as a dessert topping
e. for protein purification

An enzyme catalyzes the reaction S → P. The table shows how the reaction rate (v) of the enzyme varies with the substrate concentration [S].

a) Create a Lineweaver-Burk plot of the data given in the table above.
b) Calculate Km, Vm, and Vm / Kmfor the enzyme.
c) Also calculate kcat and kcat / Km (the specificity constant) when given that
  [E] = 10 nM.d) How saturated will an enzyme be if the activity is measured at a substrate concentration 2x greater than Km? Give the answer as a percentage of Vm.

1. What is a multi-enzyme complex? What are the advantages of a multi-enzyme complex?

2. What is the function of each of the three catalytic enzymes that make up pyruvate dehydrogenase? What is the role of prosthetic groups TPP and lipoic acid and which enzyme is each attached to?

3. What are the substrates and the products of the steps in the Citric Acid Cycle where CO₂, NADH, and FADH₂ are produced?

next to each statement it is true or false

The 1.-An enzyme can only function once, because it is changed by the chemical reaction. [ Select ]

2.- An enzyme's function depends on its three-dimensional shape. [ Select ]

3.- Each enzyme can work with a broad range of substrates. [ Select ]

4. An enzyme inhibitor can prevent a substrate from binding to the active site. [ Select ]

3)   In enzyme kinetics why does the initial reaction rate (vo) resemble the steady state in living cells?  

4)   Also, in enzyme kinetics the Km value is an indicator of enzyme binding efficiency, is a low or high Km value indicative of better efficiency in living cells? Why?

5)   Consider competitive inhibitors. Why does their presence raise the Km value?

Are the following acids, bases, or neutral? NaNO₂​, HNO₂, NaC₂H₃O₂​. Please also explain why they are acids or bases. i.e. how do i know if they are proton donors or acceptors?

Red blood cells in the lungs are sufficiently oxygenated to carry out aerobe glycolysis. Why do they, however, metabolize glycose to lactate?

3. Why is it possible for fructose, galactose, mannose and even glycerol to be catabolized via glycolysis? Provide specific explanation for each compound