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.
Make Your Own Quizzes and Flashcards
Convert your notes into interactive study material.
Get started for free
