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Alanine is the simplest α-amino acid after glycine. The methyl side-chain of alanine is non-reactive and is therefore hardly ever directly involved in protein function. [12] Alanine is a nonessential amino acid, meaning it can be manufactured by the human body, and does not need to be obtained through the diet. Alanine is found in a wide ...
For example, the systematic name of alanine is 2-aminopropanoic acid, based on the formula CH 3 −CH(NH 2)−COOH. The Commission justified this approach as follows: [7] The systematic names and formulas given refer to hypothetical forms in which amino groups are unprotonated and carboxyl groups are undissociated.
The Alanine World Hypothesis postulates that the evolution of the genetic code (the so-called GC phase [87]) started with only four basic amino acids: alanine, glycine, proline and ornithine (now arginine). [88] The evolution of the genetic code ended with 20 proteinogenic amino acids.
β-Alanine (beta-alanine) is a naturally occurring beta amino acid, which is an amino acid in which the amino group is attached to the β-carbon (i.e. the carbon two carbon atoms away from the carboxylate group) instead of the more usual α-carbon for alanine (α-alanine). The IUPAC name for β-alanine is 3-aminopropanoic acid.
Amino acid biosynthesis overview. The drawn molecules are in their neutral forms and do not fully correspond to their presented names. Humans can not synthesize all of these amino acids. Amino acid biosynthesis is the set of biochemical processes (metabolic pathways) by which the amino acids are produced.
Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion. Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may ...
However, additional molecular interactions may render the amide form less stable; the amino group is expelled instead, resulting in an ester (Ser/Thr) or thioester (Cys) bond in place of the peptide bond. This chemical reaction is called an N-O acyl shift. The ester/thioester bond can be resolved in several ways:
Only proline differs from this basic structure as its side chain is cyclical, bonding to the amino group, limiting protein chain flexibility. [34] The side chains of the standard amino acids have a variety of chemical structures and properties, and it is the combined effect of all amino acids that determines its three-dimensional structure and ...