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Glutamine is one of the twenty amino acids which are needed by the body of humans and animals to function properly. The molecular formula of Glutamine is C5H10N2O3 and it is abbreviated as ‘Gln’ or even as ‘Q’. This element is vital in the synthesis of protein, donation of carbon and nitrogen and for cellular energy as well as for the functioning of the kidney. Glutamine also helps in maintaining the acid-base balance in the kidneys by producing a sufficient amount of NH4 (ammonium). The living system characteristically uses the simple sugar glucose, but when it is not available, glutamine is used.
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Key Terms: Glutamine, Amino Acids, Proteins, Glucose, Cellular Energy, Adenosine Triphosphate, Carboxylic Group
What is Glutamine?
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Glutamine is one of the non-essential amino acids which is encoded by CAA & CAG and is a conditional-essential amino acid (in situations such as gastrointestinal disorders or intensive athletic training). The IUPAC name of C5H10N2O3 is Glutamine. Glutamine has one carboxyl group and one amino group with the amide group in the side-chain of the carboxyl group.
Amino acids that are present in our body can be classified into two types:
- The Essential Amino Acids: The ones which are very much necessary in the diets as the body does not synthesize them or build them for any other chemicals.
- The Non-Essential Amino Acids: The ones synthesized by the body from other chemicals and are also a dietary source.
Glutamine is a precursor to cell energy, adenosine triphosphate (ATP) and vital to protein synthesis. This means that it is essential in making proteins. Without glutamine, a protein won’t fold correctly or function properly and disease or death can happen if a protein is not able to fold correctly.
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Structure of Glutamine
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Glutamine is mostly a linear molecule that behaves as a polar molecule having positive (+ve) and negative (-ve) charges. The side chain of glutamine is known as a simple amide or amino group – NH2, located in the end region of the R-group. This consists of another group called the carboxylic group (on the other end of the carbon atom). The amino acid is considered to be hydrophilic as it is polar in nature.
Structure of Glutamine
Read More: Glutamic Acid
Glutamine consists of other 2-molecules with the use of an enzyme called glutamine synthetase namely;
- Glutamate
- Ammonia.
This is mostly done in the muscles, brain tissues, liver and sometimes in the lungs.
How Does Glutamine Function?
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The human body synthesises amounts of glutamine which are used in various biological processes, like the metabolic processes taking place in the kidney, liver, etc. Glutamine has the capability of donating carbon (C) and nitrogen (N) atoms that are important for various mechanisms like anabolic, metabolic, cell division, etc. Glutamine, unlike many chemicals, has the highest amount of concentration of free-floating amino acid in the blood and can also cross the blood-brain barrier.
An anabolic process is where energy is needed in order to make a new chemical in biochemistry. A typical process in humans is the production of purines (one of the four base pairs of deoxyribonucleic acid (DNA). But this requires extra energy, so the amide group is removed and added to other chemical constituents to make purine. Glutamine can also donate carbon (C) and is a vital source of carbon within the last half of energy metabolism. The second half of energy metabolism is called the citric acid cycle, where adenosine triphosphate (ATP) is made.
Sources of Glutamine
Read More: Krebs Cycle
Functions and Uses of Glutamine
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Some of the functions of Glutamine are as follows:
- Glutamine helps the body in the formation of energy and this amino acid is said to be the highest concentration of a free-floating amino acid in the blood.
- It helps in the synthesis of proteins in the body and regulates the acid-base balance within the kidneys by producing enough ammonium.
- Glutamine helps in the synthesis of lipids in the cancer cells.
- This amino acid plays a vital role when related to stress which is caused by trauma, burns, excessive exercise and various diseases like cancer very often resulting in glutamine deficiency.
- It also helps to develop supplements helping the body to recover from stress.
Read More: Difference between Essential and Non-essential Amino Acids
Things to Remember
- The IUPAC name of C5H10N2O3 is glutamine and is abbreviated as ‘Gln’ or even as ‘Q’.
- Glutamine is one of the non-essential amino acids and is a linear molecule that behaves as a polar molecule.
- Glutamine has the capability of donating carbon (C) and nitrogen (N) atoms that are important for various mechanisms.
- This amino acid plays a vital role when related to stress which is caused by trauma, burns, and excessive exercise.
- It helps in the synthesis of proteins in the body and regulates the acid-base balance.
Important PYQs Based On Glutamine
- Out Of The Following Which Type Of Interaction Is
- The Helical Structure Of Protein Is Stabilized By
- Which Of The Following Is A Fibrous Protein
- The Prosthetic Group Present In Glycoproteins Is
- In Fibrous Proteins Polypeptide Chains Are Held To
- Protein Is A Polymer Of
- Pleated Sheet Structure Of Protein Shows Maximum
- Which One Of The Following Is A Conjugated Protein… [BCECE 2007]
- The Protein Present In The Hair Is
- In The Following Reaction Acetamide P 2o 5 Y H 2o
- Hofmann Bromamide Degradation Reaction Is Shown By
- Hofmann Degradation Of Benzamide Gives Aniline Hof
- Acidic Hydrolysis Of Acetamide Gives
- Which Of The Following Is A Polyamide
- Hofmann S Bromamide Reaction Is Used To Convert
- 59 G Of An Amide Obtained From A Carboxylic Acid R
- When Acetamide Is Hydrolysed By Boiling With Acid
- When Acetamide Is Treated With Br 2 And Caustic So
- Hoffmann S Bromamide Reaction Is Used To… [JKCET 2017]
- An Alkyl Cyanide Forms An Amide When It Is Treated [AMUEEE 2011]
Sample Questions
Ques. What foods are sources of glutamine? (3 Marks)
Ans. Animal proteins including beef, poultry, pork, fish and organ meats are sources of glutamine. Meat is one such food that has a very high amount of protein. Any food that is high or rich in protein is considered to be high in glutamine. Hence, meat is considered one of the richest sources of glutamine. As a result, beef, chicken and lamb are excellent sources of glutamine.
Ques. Why are amino acids called amphoteric? (2 Marks)
Ans. Amino acids have both acidic and basic properties, this is why they are amphoteric. The pH of the solutions determines the predominant form of the amino acid.
Ques. What is the difference between glutamine and L-glutamine? (3 Marks)
Ans. The key difference between glutamine and L-glutamine is:
Glutamine is an amino acid, whereas, on the other hand, L-glutamine is an isomer of glutamine. There are two types of isomers of glutamine namely L-glutamine and D-glutamine. L-glutamine is found in abundance in the body and participates in various functions. Beef, chicken, fish, milk, cabbage, beets, beans, spinach, eggs, and parsley are dietary sources of L-glutamine.
Ques. Define amino acids. (3 Marks)
Ans. Amino acids can be defined as the organic compounds containing the basic amino groups (-NH2) and carboxyl groups (-COOH).
Basically, there are two types of amino acids in our body:
- The essential amino acids: The ones which are very much necessary in the diets as the body does not synthesize them or build them for any other chemicals. The nine essential amino acids are Isoleucine, lysine, leucine, phenylalanine, histidine, tryptophan, methionine, threonine, and valine.
- The non-essential amino acids: The ones synthesized by the body from other chemicals and are also a dietary source. For example, aspartic acid, glutamic acid, alanine, glycine, tyrosine, serine, etc.
Ques. Write the molecular formula of glutamine. (3 Marks)
Ans. Glutamine has the molecular formula C5H10N2O3 . It is usually a linear molecule which behaves as a polar molecule having positive (+ve) and negative (-ve) charges. The side chain of glutamine is known as a simple amide or amino group – NH2, located in the end region of the R-group. This consists of another group called the carboxylic group (on the other end of the carbon atom). The amino acid is considered to be hydrophilic as it is polar in nature.
Ques. Is glutamine a conditionally essential amino acid? (3 Marks)
Ans. Glutamine is an existing amino acid in our body and is also the most abundant amino acid present in the human body. It is a conditionally essential amino acid. It means that if there is an ill or stressed person, then, he/she may not be able to produce Glutamine on their own. Glutamine production happens in the muscles.
Ques. How does glutamine benefit athletes? How many doses of glutamine are recommended every day? (3 Marks)
Ans. Glutamine helps in recovering the muscles faster for athletes and in strengthening the immune system, which helps in the improvement of weakened immune systems through intense exercises. On average, a dose of 20-30 grams, is suggested for an adult with a normal activity rate. But for intense exercising, weightlifting, athletics, etc. then more dose of it is needed to regulate the relaxation and recovery of your muscles.
Ques. What are the uses of glutamine? (4 Marks)
Ans. Glutamine helps in the synthesis of proteins and the formation of energy in the human body. Glutamine helps in synthesizing lipids in the cancer cells. It helps in the synthesis of proteins in the body and regulates the acid-base balance within the kidneys by producing enough amount of ammonium.
This amino acid plays a vital role when related to stress which is caused by trauma, burns, excessive exercise and various diseases like cancer very often result in glutamine deficiency. Apart from that, Glutamine also offers a number of important functions and also develops supplements helping the body to recover from stress.
Ques. Is glutamine safe? (4 Marks)
Ans. Glutamine is safe in adults and preterm infants. Glutamine is metabolized to glutamate and ammonia. Though it has some neurological effects, their concentrations are not that much. It has no adverse neurological effects. The safe level for supplemental L-glutamine in normal healthy adults is restricted to 14 g/day.
Even though glutamine has no effect on the proliferation of tumour cells, it is still possible that glutamine supplementation can be detrimental in some cancer types. Stopping the glutamine supplementation in people who are adapted to very high consumption may start a withdrawal effect by raising the risk of health problems such as infections or impaired integrity of the intestine.
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