Table of Contents
Sources Of Aspartic Acid :
Aspartic acid is a non-essential amino acid that is synthesized in the body from glutamic acid. It can also be obtained from food sources, such as meat, dairy products, eggs, nuts, and legumes. Aspartic acid is necessary for the body to make proteins and enzymes, and it also plays a role in energy production.
Aspartic acid is an acidic amino acid with functional groups of two carboxylic groups along with one amino group. There are about 20 important types of amino acids that are found in nature, more on this later. Every amino acid molecule is made up of two functional groups, they are opposite in characteristics, one is an amino group, and then there is a carboxylic acid. An aspartic acid structure is no exception; it contains one α-amino group which is in NH3+ forms and the carboxylic group that is in deprotonated –COO-. The aspartic acid formula looks like this- (C4H7NO4). Aspartic acid is a non-essential amino acid as the human body can synthesize it as it is needed. Aspartic acid can be found in a plethora of eatables including oysters, avocado, sugar beets etc.
The aspartic acid molecule is made up of two functional groups, one is an amino group, and then there is a carboxylic acid. The amino group is always on the left side when you are looking at the molecule, and the carboxylic acid is on the right. The aspartic acid molecule is also a neutral molecule, meaning it doesn’t have a net charge.
Why Is Aspartic Acid Different From Other Amino Acids?
Aspartic acid is unique from other amino acids because it can exist in either of two different forms, called isomers. The isomers are called D-aspartic acid and L-aspartic acid. The D-form is the more common isomer and is found in nature. The L-form is a mirror image of the D-form and is not found in nature.
As we previously discussed that amino acid has two functional groups, here we will dive a little deeper and shine some light on the third group, the R-group or the side chains, that gives the aspartic acid structure a distinction from the other amino acids such as glycine or cysteine. The R-group of the amino acids exerts profound changes in the biological activity of proteins. Amino acids are generally classified based on the characteristics of the functional group on the side chain in a neutral pH medium. They can be polar or nonpolar, polar yet charged, negatively charged or positively charged. The carboxyl group that is present in the side chain of the aspartic acid structure is ionized at physiological pH, which is known as aspartate, it is also from where the acid gets its name from. Glutamic acid also shares this sub-category with aspartic acid, the ionized carboxyl group in Glutamic Acid is known as glutamate.
Aspartic Acid Hybridization
In biochemistry, aspartic acid is an amino acid with the formula HOOC-CH(NH2)-COOH. It is a polar, acidic, and water-soluble molecule. In solution, it ionizes to form aspartate (CH3COO−) and hydrogen ions (H+). Aspartate is the precursor to the neurotransmitter GABA and to the amino acid asparagine.
Aspartic acid is a nonessential amino acid, meaning the body can synthesize it from other molecules. It is found in many protein-containing foods, including meat, eggs, dairy products, legumes, and nuts.
Aspartate is not always considered an amino acid. In some older textbooks, it is classified as a “dicarboxylic acid”.
