A thiol-containing non-essential amino acid that is oxidized to form cystine.
A covalently linked dimeric nonessential amino acid formed by the oxidation of cysteine. Two molecules of cysteine are joined together by a disulfide bridge to form cystine.
A non-essential amino acid, but nutritionally important since it spares the essential amino acid methionine. In addition to its role in protein synthesis, cysteine is important as the precursor of taurine, in formation of coenzyme A from the vitamin pantothenic acid and in formation of the tripeptide glutathione.
An amino acid of molecular weight (mol wt) 121 Daltons. It is incorporated in many proteins. It possesses a sulfhydryl group (SH) that makes cysteine a mild reducing agent. Cysteine can cross-link with another cysteine located on the same or on a different polypeptide chain to form disulfide bridges. The “free” cysteine group is called a thiol group.
A nonessential 3 carbon amino acid containing sulfur; can be made from methionine.
Along with methionine, the amino acid cysteine is one of the sulfur-containing amino acids required for protein synthesis. Cysteine is a nonessential amino acid because it can be synthesized from methionine. Besides production of proteins, cysteine is notably one of three amino acids that produces glutathione, which functions with glutathione peroxidase as an antioxidant.
Essential (not produced by the body, required in the diet) amino acid.
A sulfur-containing amino acid that is an important constituent of many enzymes. The disulphide (S-S) links between adjacent cysteine molecules in polypeptide chains contribute to the three-dimensional molecular structure of proteins.
An amino acid joined with another cysteine amino acid to create cystine amino acid.