Exam 7: Kinetics and Regulation

Choose the correct answer from the list below. Not all of the answers will be used. -_______________: A complex array of enzyme reactions organized in multiple pathways.

Loss of allosteric regulation in the production of purine nucleotides results in:

Allosteric effectors:

When designing a drug to inhibit the formation of a product which requires several enzymes in a metabolic pathway, what should be the first piece of information a biochemist needs to develop the drug?

What is the upper limit of k_cat/K_M?

Choose the correct answer from the list below. Not all of the answers will be used. -_______________: The study of rates of chemical reactions.

Homotrophic effects of allosteric enzymes:

A protease hydrolyzes the peptide backbone.What is/are the substrate(s) and product for this reaction? Assuming that the concentration of water is so high (~55M) that it does not appreciably change, to what kind of reaction order would one assign this reaction?

When [S] << K_M, the enzymatic velocity depends on:

An allosteric ______________ stabilizes the T state of the enzyme.

Reactions that have more two reactants or substrates are considered ______________ reactions.

Allosteric enzymes can be identified because the plot of initial velocity, V0, versus substrate concentration, S, is not hyperbolic but ______________ shaped.

Choose the correct answer from the list below. Not all of the answers will be used. -At _______________, there is no net change in the concentration of substrate or product.

Choose the correct answer from the list below. Not all of the answers will be used. -The value V0 is called the _______________.

Allosteric proteins:

Multiple substrate enzyme reactions are divided into two classes:

Choose the correct answer from the list below. Not all of the answers will be used. -_______________: Enzymes that do not obey Michaelis-Menten kinetics.

One way to measure the rate of an enzymatic reaction is to measure the loss of ______________ over time.

Which of the following is true under these conditions: The enzyme concentration is 5 nM, the substrate concentration is 5 mM, and the K_M is 5 μM.

When a substrate concentration is much greater than KM, the rate of catalysis is almost equal to: