Question

1.     Oxaloacetate can be converted into several different metabolic compounds. Briefly discuss each one, and include whether that is part of a catabolic or anabolic pathway.

2.     There are several allosteric regulators of pyruvate carboxylase. For each one, explain the following:

o   Is this molecule an allosteric activator or allosteric inhibitor?

o   Why does it make sense that it would regulate the enzyme in that way?

o   Does this inhibitor/activator stabilize the R state or T state of the enzyme?

Acetyl CoA

Aspartate

3.     Draw a Michaelis Menten graph to represent normal pyruvate carboxylase kinetics. Explain why you drew things as you did.

A deficiency in pyruvate carboxylase is a rare autosomal recessive inborn error in metabolism. The most severe form is called Type B or French phenotype

4. Explain why a deficiency in pyruvate carboxylase would result in the following metabolic issues:

o   State the specific pathway(s) that produces the condition. For example, answer glycolysis instead of just glucose metabolism.

o   Explain why this pathway would be involved during pyruvate carboxylase deficiency.

a.     Lactic acidemia, with an elevated lactate to pyruvate ratio

b.     Ketoacidosis

c.      Hypoglycemia

d.     Hyperammonemia

e.     Hypercitrullinemia

A milder form of the disease is Type A. These individuals only have mild lactic acidemia and psychomotor retardation and live longer, though some die within a few years. One of the mutations that causes Type A is a mutation from Alanine to Threonine at amino acid 610, located within the pyruvate binding domain

5.     Draw the predominant form of the amino acids alanine and threonine at the following pH values.

pH 7: alanine and threonine

pH 4: alanine and threonine

6.     What non-covalent interactions can each amino acid participate in, as part of tertiary structure at pH 7?

Suggest one amino acid whose side chain can participate in a non-covalent interaction with the side chain of alanine, and one amino acid whose side chain can participate in a non-covalent interaction with the side chain of threonine.

Include an explanation of the charges involved in the interaction: full or partial charges? Are the charges permanent or temporary?

Alanine

Threonine

7.     Let’s assume that this amino acid is on the surface of the protein. Would you expect this mutation (alanine mutated to threonine), to have any effect on the three-dimensional shape of the protein? Explain your reasoning.

8.     What is your topic of choice? A topic could be a metabolic pathway, a disease, an enzyme, a biochemical principle (ex. hydrophobic effect, enzyme properties), a thermodynamic principle (ex. Entropy), etc.

a.      What is the topic and why did you choose this topic?

To learn more about the topic, consult your textbook and also find 2 references (primary or secondary) published in the last 10 years and write a paragraph. Cite your sources.

b.     Why would this topic be of interest to non-science majors? Explain how would you teach a key idea to someone who does not have a science background. Your answer should include what you would actually say to that person. You may include images (cite sources)

c.      Suppose you have a friend who is a science major and must take this course next semester. How would you explain a key idea of your topic to that friend? Your answer should include what you would actually say to that friend. Images can be posted too.

Answer 1

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