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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 variety of foods, but is particularly concentrated in meats.
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.
These six are alanine, aspartic acid, asparagine, glutamic acid, serine, [2] and selenocysteine (considered the 21st amino acid). Pyrrolysine (considered the 22nd amino acid), [ 3 ] which is proteinogenic only in certain microorganisms, is not used by and therefore non-essential for most organisms, including humans.
Alanine transaminase (ALT), also known as alanine aminotransferase (ALT or ALAT), formerly serum glutamate-pyruvate transaminase (GPT) or serum glutamic-pyruvic transaminase (SGPT), is a transaminase enzyme (EC 2.6.1.2) that was first characterized in the mid-1950s by Arthur Karmen and colleagues. [1]
Alanine and Cori cycles. The Cahill cycle, also known as the alanine cycle or glucose-alanine cycle, [1] is the series of reactions in which amino groups and carbons from muscle are transported to the liver. [2] It is quite similar to the Cori cycle in the cycling of nutrients between skeletal muscle and the liver. [1]
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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.
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