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Lysine and threonine do not undergo transamination because they do not possess the alpha-amino group that is required for the transamination process to occur. Transamination involves the transfer of an amino group from an amino acid to an alpha-keto acid, forming a new amino acid. Since lysine and threonine lack the necessary amino group, they cannot participate in transamination reactions.
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What type of reaction is aspartic acid plus α-ketoglutaric acid equals glutamic acid plus oxaloacetic acid?
This reaction is a transamination reaction, where the amino group from aspartic acid is transferred to α-ketoglutaric acid to form glutamic acid and oxaloacetic acid. Transamination reactions are important for amino acid metabolism and synthesis.
Metabolic importance of transamination reactions?
Transamination reactions are important for converting one amino acid into another by transferring an amino group. This process is crucial for amino acid metabolism, as it allows for the synthesis of non-essential amino acids and the breakdown of excess amino acids. Transamination also plays a key role in the urea cycle, helping to eliminate nitrogen waste from the body.
What is the pH of Lysine?
Lysine itself is a neutral compound and therefore does not have a pH value. When lysine is dissolved in water, the pH of the solution will depend on the concentration of lysine and other substances present in the solution.
How does Serine form a bond with Lysine?
Serine can form a bond with lysine through a hydrogen bond or an electrostatic interaction between the hydroxyl group of serine and the amino group of lysine. This interaction can occur in proteins and peptides where serine and lysine are in close proximity within the molecular structure.
What scientist discovered lysine?
The discovery of lysine is attributed to two scientists, Emil Abderhalden and Albert Windaus. Abderhalden, a Swiss biochemist, first identified lysine in 1902, while Windaus, a German chemist, further characterized its chemical structure in the early 20th century.
Where does lysine bond another lysine?
i just came across a lysine-lysine bond in a b-barrel n-termini fragment that's embedded in the membrane
Is rice rich in lysine?
Yes, it is rich in lysine.
Is lysine an enzyme?
No. Lysine is an amino acid. Amino acids are the building blocks of proteins.
In transamination the amino group of an amino acid is?
transferred to a keto acid
What alpha-keto acid produce when alanine undergoes transamination?
Pyruvate
What type of reaction is aspartic acid plus α-ketoglutaric acid equals glutamic acid plus oxaloacetic acid?
This reaction is a transamination reaction, where the amino group from aspartic acid is transferred to α-ketoglutaric acid to form glutamic acid and oxaloacetic acid. Transamination reactions are important for amino acid metabolism and synthesis.
Metabolic importance of transamination reactions?
Transamination reactions are important for converting one amino acid into another by transferring an amino group. This process is crucial for amino acid metabolism, as it allows for the synthesis of non-essential amino acids and the breakdown of excess amino acids. Transamination also plays a key role in the urea cycle, helping to eliminate nitrogen waste from the body.
What are the two amino acids that jello lack?
tryptophan and lysine lysine
Is olive oil high in lysine?
Olives or olive oil is not renowned as a source of lysine. Beans and pulses are the usual vegetable sources of lysine.
What is the pH of Lysine?
Lysine itself is a neutral compound and therefore does not have a pH value. When lysine is dissolved in water, the pH of the solution will depend on the concentration of lysine and other substances present in the solution.
Does lysine help you lose weight?
I don't believe lysine helps you to lose weight. I believe lysine is a preventive for fever sores such as from the sun. CG
What is the process in which a amino group is combined with a keto acid to form an amino acid?
Transamination
