Problem 31
You do an enzyme kinetic experiment and calculate a \(V_{\max }\) of 100 \mumol of product per minute. If each assay used \(0.1 \mathrm{mL}\) of an enzyme solution that had a concentration of \(0.2 \mathrm{mg} /\) \(\mathrm{mL},\) what would be the turnover number if the enzyme had a molecular weight of \(128,000 \mathrm{g} / \mathrm{mol}\) ?
Problem 32
The enzyme D-amino acid oxidase has a very high turnover number because the \(\mathrm{p}\) -amino acids are potentially toxic. The \(K_{\mathrm{M}}\) for the enzyme is in the range of 1 to \(2 \mathrm{m} M\) for the aromatic amino acids and in the range of 15 to \(20 \mathrm{m} M\) for such amino acids as serine, alanine, and the acidic amino acids. Which of these amino acids are the preferred substrates for the enzyme?
Problem 35
Why does acetazolamide make beer taste flat?
Problem 39
What are the three most common mechanisms for enzymecatalyzed reactions that have two substrates?
Problem 46
If we describe an enzyme like aspartate transcarbamoylase and say that it exhibits cooperativity, what do we mean?
Problem 47
How can competitive and pure noncompetitive inhibition be distinguished in terms of \(K_{\mathrm{M}}\) ?
Problem 50
Distinguish between the molecular mechanisms of competitive and noncompetitive inhibition.
Problem 52
Why is a Lineweaver-Burk plot useful in analyzing kinetic data from enzymatic reactions?
Problem 53
Where do lines intersect on a Lineweaver-Burk plot showing competitive inhibition? On a Lineweaver-Burk plot showing noncompetitive inhibition?
Problem 57
Why does the apparent \(K_{\mathrm{M}}\) decrease in the presence of an uncompetitive inhibitor?
