why is asparagine has two nitrogen atoms and aspartic acid as one
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1_ ASPARAGINE:_
Asparagine is found in abundance in asparagus, and is thus named so. Asparagine is not an essential amino acid, meaning that it is not necessary for humans to ingest it to receive necessary amounts. Asparagine has a high propensity to hydrogen bond, since the amide group can accept two and donate two hydrogen bonds. It is found on the surface as well as buried within proteins. It is a common site for attachment of carbohydrates in glycoproteins. Food sources that contain asparagine is dairy, beef, poultry, and eggs.
Features:_
Asparagine is not an essential amino acid, meaning that it is not necessary for humans to ingest it to receive necessary amounts. Asparagine has a high propensity to hydrogen bond, since the amide group can accept two and donate two hydrogen bonds. It is found on the surface as well as buried within proteins. It is a common site for attachment of carbohydrates in glycoproteins.
Functions:_
Asparagine is required by the nervous system to maintain equilibrium and is also required for amino acid transformation from one form to the other which is achieved in the liver.
Synthesis:_
Synthesis of asparagine requires oxaloacetate, C4H4O5. The double bonded oxygen attached to carbon-2 is replaced by ammonium group from glutamate via a process called transaminase. The newly formed compound, or aspartate, is converted to asparagine by replacing a negatively charged oxygen end with an ammonium group. The asparagine synthesis converts glutamine to glutamate, and ATP into AMP and pyrophosphate.
Analysis:_
Asparagine can be identified by following methods: UV spectrometry, infrared spectroscopy (IR), nuclear magnetic spectroscopy, (NMR), and mass spectroscopy.
2_ ASPARTIC ACID:_
Also known as aspartate, Aspartic acid is an acidic and polar amino acid that has carboxylic acid group, which loses a proton to be carboxylate group for physiological pH and has a negative charge; the carboxylic acid group of the amino acid has a pKa value of 4.1, which is a little basic than the terminal α-carboxyl group. Its pI is 5.41. Proteins are critical to maintain the pH balance in the body.
Features:_
Aspartic acid is a non-essential amino acid can be obtained from central metabolic systems.
Functions:_
Aspartic acids are involved in transamination in which oxaloacetate and aspartate is interconvertible. It is also involved in immune system activity by promoting immunoglobulin production and antibody production. Moreover, aspartic acid protects the liver and helps in detoxification of ammonia.Other than its role as an excitatory neurotransmitter, aspartate is proteinogenic amino acids that are used in coding of DNA.
Other than its role as an excitatory neurotransmitter, aspartate is proteinogenic amino acids that are used in coding of DNA.Aspartate plays important roles as acids in enzyme active centers, as well as in maintaining the solubility and ionic character of proteins.
Synthesis:_
Aspartic acid is synthesized from oxaloacetate via transamination. Aspartic acid can be used as an initial reactant in synthesis of other essential amino acids as well: methionine, threonine, isoleucine, and lysine. Aspartic acid needs to be reduced to its semialdehyde form of HOOCCH(NH2)CH2CHO. Asparagine can be also obtained from aspartic acid via transamidation: aspartic acid + glutamine -> asparagine + glutamic acid
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