Chemistry Questions

Outline and briefly describe the fate of proteins degraded in carnivores.

What is a protease and why are they produced and secreted as zymogens?

List the common characteristics of aminotransferases or transaminases.

In humans, where do ingested proteins become broken down into respective amino acids?

How are SGPT and SGOT (and creatine kinase) useful diagnostic enzymes?

Describe the reaction catalyzed by glutamate dehydrogenase and briefly provide a rationale behind the direction of the allosteric control by ADP and GTP.

PLP primarily plays a role as a coenzyme in the metabolism of molecules bearing amino groups. In what other metabolic reactions does it act as a coenzyme?

Describe the roles of glutamine and glutamate in amino group metabolism and transport.

Glutamate dehydrogenase works on glutamate in the liver. What two products does this reaction yield?

How and under what circumstances does the kidney play a role in glutamine processing?

List the four metabolites in the urea cycle that must cross the mitochondrial membrane.

In the urea cycle, from where does aspartate get its amino group?

Why is the urea cycle such an energy expensive process?

What role does glutamate play in the central nervous system?

Explain how the degradation of amino acids feeds into the central catabolic processes of the cell.

List the amino acids that are degraded to α-ketoglutarate?

a) List the amino acids ultimately converted to acetyl-coA.

b) Tryptophan catabolism can yield acetyl-coA via two different pathways. List three other important biomolecules derived from intermediates of tryptophan breakdown.

Which reaction pathway converts the carbon skeleton of alanine to a ketone body?

How, specifically, is the branched-chain amino acid dehydrogenase complex regulated, and where may it be found?

What is the fundamental difference between keto-genic amino acids and glucogenic amino acids?

Organisms are constantly trying to achieve homeostasis, and the effects of amino acid oxidation and the production of urea are not limited to a single physiological system. Locate the following article and answer the questions below:

Chan H, and Butterworth R. (2003) Neurochemistry International, 43 (4,5): 525-532.

a)  Increased brain ammonia leads to cerebral swelling via what mechanism?

b)  An increase in the presence of ammonia in the brain is often identified concomitant with increased extracellular concentrations of glutamate. T/F

Select one of the disorders listed in table 18-2. Using information in your text and online, elaborate on the condition with respect to the specific defective enzyme (or complex) and process, relating them to the symptoms and effects.

Read the following article and answer the associated questions:

Townsend DM, Tew KD, and Tapiero H. (2004) Biomedicine and Pharmacotherapy, 58 (1): 47-55.

a)  In the conversion of dietary amino acid methionine to cysteine, a component of the antioxidant glutathione and precursor to taurine, what enzyme catalyzes the first step in this reaction?

(Note that a deficiency of this enzyme leads to clinically recognized hypermethioninemia.)

b)  Birth defects have been associated with high levels of maternal homocysteine. How does administration of folic acid serve to protect the fetus?

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