Serine

Serine is a protein-building amino acid with a hydroxyl-bearing side chain. It is polar and usually nonessential in human nutrition.

Amino acid: An organic molecule with amino and carboxyl groups; amino acids are the building blocks of proteins. Serine is one of the standard amino acids used to build proteins.
Phosphorylation: The addition of a phosphate group to a molecule, often a protein. Protein kinases commonly attach phosphate to serine’s side-chain hydroxyl.
Proteinogenic amino acid: An amino acid encoded by the genetic code and incorporated into proteins during translation. Serine is directly encoded in the genetic code and incorporated into proteins.
Threonine: A protein-building amino acid with a polar hydroxyl-bearing side chain and an essential dietary requirement in humans. Like serine, it has a hydroxyl side chain, but humans must obtain it from food.
Hydroxyl group: An oxygen–hydrogen functional group written as –OH. Serine’s side-chain hydroxyl makes it polar and chemically reactive.
O-linked glycosylation: A protein modification that attaches a sugar to the oxygen atom of an amino-acid side chain. Serine’s hydroxyl can anchor O-linked sugars in proteins.
Phosphoproteomics: The large-scale study of phosphorylated proteins and their modification sites. It measures serine phosphorylation, a common regulatory protein modification.
Alanine: A protein-building amino acid with a small, nonpolar methyl side chain. Its nonpolar side chain contrasts with serine’s water-interacting hydroxyl group.
Polar amino acid: An amino acid whose side chain interacts favorably with water or other polar molecules. Serine belongs to this class because its side chain contains a hydroxyl group.
Serine protease: A protease that uses a serine residue in its active site to cleave peptide bonds. Its reactive serine performs the central nucleophilic step in peptide-bond cleavage.

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