Amino Acid Transamination Reactions Quiz

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18 Questions

What is the purpose of transamination?

To collect amino groups to form glutamate

Which enzyme is responsible for the formation of ammonia from glutamate?

Glutamate dehydrogenase

Which vitamin derivative is the prosthetic group of all transaminases?

Vitamin B6 (Pyridoxine)

Where does the oxidative deamination of glutamate occur?

Mitochondria

Which of the following is a product of the reaction: Ala + KG → Pyruvate + Glutamate?

Pyruvate + Glutamate

Why is it important to prevent NH4+ buildup in tissues?

To ensure proper urea formation in the liver

What is the main function of transaminases or amino transferases?

Synthesis of non-essential amino acids

During transamination, what happens to the α-amino group of an amino acid?

It is enzymatically removed and transferred to an α-carbon atom of an α-keto acid

Which process involves the amination of α-ketoglutarate?

Transamination

What is the final excretory group formed when amino groups are not re-used?

Urea

Which enzyme promotes the removal of the amino group during transamination?

Alanine transaminase

What happens to the α-keto acid during transamination?

It forms an α-amino acid analog

What is the primary function of transaminases in amino acid metabolism?

To funnel amino groups from various compounds

Which enzyme converts alanine to pyruvate?

Alanine Transaminase

In amino acid metabolism, where do most amino groups get funneled into?

Formation of glutamate or aspartate

Which enzyme must produce glutamine in order to lead to the urea cycle?

Glutamine Synthetase

What is the final product of the reaction catalyzed by Glutamate Dehydrogenase?

Glutamate

Which compound is a common amino group donor to the urea cycle?

Aspartate

Test your knowledge of amino acid transamination reactions involving alanine and glutamate. Identify the substrates, products, and enzymes involved in these reactions. Understand the reversibility of transaminase reactions.

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