What is Glutamine Definition Structure Formula and Uses
The essential amino acids are the ones that cannot be synthesised by our bodies. These essential amino acids have to be a part of our diet necessarily because these cannot be built from other chemicals present in our bodies. On the contrary, on-essential amino acids are the ones that can be synthesised by our bodies from other chemicals and are a dietary source.
Glutamine is one of the non-essential amino acids that are required by our body. Glutamine is encoded by CAA and CAG. It is the conditional-essential amino acid that is required in a few situations like gastrointestinal disorders or intensive athletic training. Glutamine has one carboxyl group, one amino group and one amide group in the sidechain of the carboxyl group.
What Is Glutamine?
Glutamine is an integral element which is related to stress. The stress that is caused by trauma, excessive exercise, burns, and several diseases like cancer often results in a deficiency of glutamine in the body. Glutamine is required to perform a number of functions in the body, and it also helps to build a supplement to help the body recover from the stress.
The molecular formula of Glutamine is C5H10N2O3, and it is abbreviated as ‘Gln’ or ‘Q’. This is an important amino acid and is one of the twenty amino acids that are required by human beings and the animals for proper functioning. Glutamine is an important element that is involved in the synthesis of protein, donation of carbon as well as nitrogen for the cellular energy and also for the proper functioning of the kidney. The structure of glutamine is what makes it such a vital amino acid.
Structure of Glutamine
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In general, all amino acids have an equivalent structure: an amino attached to a hydrogen, a carboxyl, and a sidechain group, denoted by ‘R’ via a central carbon. The amino and carboxyl groups and central carbon are considered the amino acid backbone and are the same in all amino acids. It is the side chain that is specific to each amino acid.
The specific structure of glutamine is indicative of its chemical formula, C5H10N2O3. The side chain or R group of glutamines is a simple amide, NH2; located at the tail end of the R group. Glutamine is a linear molecule and polar in nature that means that it has both positive and negative charges. Polar means the glutamine molecule is both positive and charged. This amino acid is water-loving because of this polar characteristic.
In general, glutamine is made from two other molecules glutamate and ammonia using an enzyme called glutamine synthetase. This is commonly done in muscles but is also in lung and brain tissue and the liver.
Nomenclature of Glutamine
The IUPAC name of C5H10N2O3 is glutamine. The name according to the nomenclature for the structure of C5H10N2O3 is L-Glutamine (levo) glutamide 2, 5 - Diamino - 5 - oxopentanoic acid, 2-Amino-4-carbamoyl butanoic acid.
Glutamine Function
The human body further synthesises more amounts of glutamine which is used in various biological processes. It is used in the metabolic processes taking place in the kidney, liver, etc. glutamine has the capacity of donating carbon and nitrogen atoms that are important for several processes like anabolic, metabolic, cell division, etc.
This amino acid also helps in maintaining the acid-base balance in the kidneys by producing an ample amount of ammonium. It also helps in the synthesis of lipids in the cancer cells.
Glutamine acid is vital to protein synthesis. This means that this amino acid is essential in making proteins. Without glutamine, a protein won’t fold correctly or function properly. If a protein is not able to fold correctly, disease or death can happen. If a protein folds but cannot function thanks to a change in amino alkanoic acid structure, death also can occur.
Glutamine is a precursor to cell energy, adenosine triphosphate (ATP). The living system typically uses the simple sugar glucose, but when glucose is not available, glutamine is used. Glutamine is the highest concentration of free-floating amino acid in the blood and can cross the blood-brain barrier, unlike many chemicals. This is in addition to its part in energy formation.
Glutamine, under special conditions, can donate nitrogen. An anabolic process is a process where energy is needed to make a new chemical in biochemistry. A typical process in humans is the production of purines or one of the four base pairs of deoxyribonucleic acid (DNA). This requires extra energy, but the amide group is removed and added to other chemical constituents to make purine.
Glutamine can also donate carbon and is a crucial source of carbon within the last half of energy metabolism. The second half of energy metabolism is called the citric acid cycle where ATP is made. The carbon groups from the R group of glutamine are often wont to form ATP to make sure of energy for all times.
Solved Problems
Question 1. How does glutamine benefit athletes?
Answer: Glutamine helps in recovering the muscles faster for the athletes. It also helps in strengthening the immune system, which helps in the betterment of weakened immune systems by intense exercises.
Question 2. How many doses of glutamine should a person take every day?
Answer: On average, a dose of 20-30 grams is suggested for an adult with normal activity rate. But if you’re into intense exercising, weightlifting, athletics, etc. then you’ll need more dose of it to regulate the relaxation and recovery of your muscles.
FAQs on Glutamine in Chemistry Structure Formula and Functions
1. What is glutamine in chemistry?
Glutamine is a polar, uncharged α-amino acid with the molecular formula C5H10N2O3. It contains an α-amino group (–NH2), an α-carboxyl group (–COOH), and a side chain with an amide functional group (–CONH2). In aqueous solution at physiological pH, glutamine exists mainly as a zwitterion with –NH3+ and –COO- groups. It is classified as a proteinogenic amino acid and is commonly abbreviated as Gln or the one-letter code Q.
2. What is the structural formula of glutamine?
The structural formula of glutamine is HOOC–CH(NH2)–CH2–CH2–CONH2. Key structural features include:
- An α-carbon bonded to –NH2, –COOH, –H, and a side chain.
- A side chain containing an amide functional group (–CONH2).
- Two nitrogen atoms: one in the amino group and one in the amide group.
3. Is glutamine acidic, basic, or neutral?
Glutamine is classified as a neutral (uncharged) polar amino acid at physiological pH. Although it contains both acidic (–COOH) and basic (–NH2) groups, its side chain is an amide (–CONH2) that does not ionize under normal biological conditions. As a result:
- The α-carboxyl group becomes –COO-.
- The α-amino group becomes –NH3+.
- The side chain remains uncharged.
4. What functional groups are present in glutamine?
Glutamine contains three main functional groups: an amino group, a carboxyl group, and an amide group. Specifically:
- α-amino group: –NH2
- α-carboxyl group: –COOH
- Side-chain amide group: –CONH2
5. What is the molar mass of glutamine?
The molar mass of glutamine (C5H10N2O3) is approximately 146.15 g·mol-1. It is calculated by summing atomic masses:
- 5 × C (12.01 g·mol-1)
- 10 × H (1.008 g·mol-1)
- 2 × N (14.01 g·mol-1)
- 3 × O (16.00 g·mol-1)
6. What is the difference between glutamine and glutamic acid?
The key difference is that glutamine has an amide side chain (–CONH2), while glutamic acid has a carboxylic acid side chain (–COOH). In detail:
- Glutamic acid (C5H9NO4) is acidic and negatively charged at physiological pH.
- Glutamine (C5H10N2O3) is neutral and uncharged at physiological pH.
7. How does glutamine form a zwitterion?
Glutamine forms a zwitterion when its amino group accepts a proton and its carboxyl group donates a proton in aqueous solution. The process involves:
- –NH2 + H+ → –NH3+
- –COOH → –COO- + H+
8. Is glutamine polar or nonpolar?
Glutamine is a polar amino acid due to its amide-containing side chain. The –CONH2 group can form hydrogen bonds with water molecules, increasing its solubility in aqueous solutions. Because it lacks a hydrocarbon-only side chain, it is not classified as nonpolar or hydrophobic.
9. What type of bond does glutamine form in proteins?
Glutamine forms peptide bonds in proteins through condensation reactions between amino acids. The peptide bond forms when:
- The –COOH group of one amino acid reacts with
- The –NH2 group of another amino acid
10. What are the chemical properties of glutamine?
Glutamine exhibits chemical properties typical of a polar, neutral α-amino acid with an amide side chain. Important properties include:
- Formation of zwitterions in aqueous solution.
- Ability to form peptide bonds in proteins.
- Hydrogen bonding due to the –CONH2 group.
- Hydrolysis of the amide side chain under strong acidic or basic conditions.
