The main difference between transamination and deamination is that in transamination, the amine group of an amino acid is exchanged with a keto group of another compound whereas, in deamination, an amino acid loses its amine group. Furthermore, in transamination, the amino acid becomes a keto acid while a deamination reaction produced ammonia. Moreover, transamination is a biochemical reaction between two molecules responsible for the synthesis of nonessential amino acids. It can occur in all types of cells of the body. In contrast, deamination is responsible for the break down of excess protein in the liver.
Transamination and deamination are two types of biochemical reactions of amino acids in the body. Enzymes catalyze both reactions.
Key Areas Covered
1. What is Transamination
– Definition, Process, Importance
2. What is Deamination
– Definition, Process, Importance
3. What are the Similarities Between Transamination and Deamination
– Outline of Common Features
4. What is the Difference Between Transamination and deamination
– Comparison of Key Differences
Key Terms
Amine Group, Amino Acids, Deamination, Nonessential Amino Acids, Transamination
What is Transamination
Transamination is a type of biochemical reaction in which an amine group (-NH2) of amino acids transfers into other molecules with a keto (C=O) group. Here, the molecules with the keto group are known as keto acids. With the exchange of the amine group and the keto group, the amino acid becomes a keto acid and the keto acid becomes a new amino acid. Therefore, transamination is a major form of biochemical reaction responsible for the synthesis of nonessential amino acids from the body.
Figure 1: Transamination
Furthermore, transamination reactions occur in all cells in the body. Also, the enzymes responsible for these reactions are transaminases or aminotransferases. The general scheme of transamination reactions, 2-oxoglutarate (α-ketoglutarate), serves as the keto acid. In addition, pyridoxal phosphate serves as the cofactor. Most of the amino acids are involved in transamination reactions except lysine, threonine, proline, histidine, tryptophan, arginine, and methionine. Especially, glutamate is the main form of amino acid produced by most transamination reactions.
What is Deamination
Deamination is another type of biochemical reaction responsible for the metabolism of amino acids. It is responsible for the removal of an amine group from amino acids, releasing ammonia. Moreover, the liver uses deamination to breakdown excess protein in the diet. Also, the deamination reactions of glutamate occur in the kidney. It is because most transamination reactions produce glutamic acid; hence, it becomes the most frequent type of amino acid which undergoes deamination.
Figure 2: Deamination
Moreover, four types of deamination reactions can occur. They are oxidative, reduction, hydrolytic, and intramolecular deamination. Oxidative deamination is the most important form of deamination reaction in higher animals. It converts the amine group of the amino acids into the corresponding keto acid while releasing ammonia. In addition, in the reduction deamination, the amino acid becomes a fatty acid. On the other hand, in the hydrolytic deamination, the amino acid converts into a hydroxy acid. In intramolecular deamination, the amino acid converts into an unsaturated fatty acid.
Similarities Between Transamination and Deamination
- Transamination and deamination are two types of biochemical reactions that occur in the body.
- They are responsible for amino acid metabolism.
- Furthermore, amine groups are subjected to both.
- Also, enzymes are responsible for catalyzing both these reactions.
Difference Between Transamination and Deamination
Definition
Transamination refers to the transfer of an amino group from one molecule to another, especially from an amino acid to a keto acid, while deamination refers to the removal of an amino group from an amino acid or other compounds. Thus, this is the main difference between transamination and deamination.
Importance
Moreover, transamination involves the synthesis of nonessential amino acids while deamination involves the breakdown of excess proteins.
Occurrence
Also, transamination occurs in all cell of the body while deamination occurs in the liver. Hence, this is another difference between transamination and deamination.
Enzymes
Furthermore, transaminases or aminotransferases are the enzymes responsible for transamination while deaminases are the enzymes responsible for deamination.
Resulting in
Their results is another major difference between transamination and deamination. Transamination results in the exchange of an amine group with a keto group while deamination results in the elimination of ammonia.
Glutamic Acid
Besides, glutamic acid is the main form of amino acid produced in transamination reactions while the primary form of amino acid which undergoes deamination is glutamic acid.
Reversibility
In addition, transamination is a reversible reaction while deamination is an irreversible reaction. So, this is also an important difference between transamination and deamination.
Conclusion
Transamination is a biochemical reaction undergone by amino acids. It is involved in the exchange of an amine group with a keto group. Transamination reactions are responsible for the synthesis of nonessential amino acids. In comparison, deamination is a biochemical reaction responsible for the breakdown of excess proteins in the liver. It involves the removal of the amine group from amino acids, releasing ammonia. Therefore, the main difference between transamination and deamination is the type of biochemical reaction and importance.
References:
1. “6.41 Transamination, Deamination & Ammonia Removal as Urea|Nutrition Flexbook.” Lumen Learning, Lumen, Available Here
Image Courtesy:
1. “Transaminierung” By Alcibiades – Own work (Public Domain) via Commons Wikimedia
2. “Deamination 5-Methylcytosine to Thymine” By Yikrazuul (talk) – Own work (Public Domain) via Commons Wikimedia
Leave a Reply