Serine: Difference between revisions

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Latest revision as of 01:49, 20 February 2025

Serine (C3H7NO3) is an amino acid that is used in the biosynthesis of protein. It contains an amino group, a carboxyl group, and a side chain consisting of a hydroxymethyl group, making it a polar amino acid. It is essential for many organisms, and can be synthesized in the human body.

Structure[edit]

Serine is a non-essential amino acid in humans (synthesized by the body), but it is vital in other organisms. It is one of the proteinogenic amino acids. The primary structure of serine is NH2-CH(COOH)-CH2-OH, and its side chain is -CH2-OH (hydroxymethyl group).

Function[edit]

Serine plays an important role in the catalytic function of many enzymes. It has been shown to occur in the active sites of chymotrypsin, trypsin, and many other enzymes. The so-called nerve gases and many substances used in insecticides have been shown to act by combining with a residue of serine in the active site of acetylcholine esterase, inhibiting the enzyme completely.

Biosynthesis[edit]

In humans, serine is synthesized from glycine or threonine. It is converted to glycine by serine hydroxymethyltransferase with tetrahydrofolate (THF) as the cofactor. Glycine can then be converted back to serine.

Dietary Sources[edit]

Serine is found in many foods, including soy, egg, chicken, beef, fish, and legumes.

See Also[edit]

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