Noun
an amino acid containing sulfur that is found in most proteins; oxidizes on exposure to air to form cystine
Source: WordNetBeta subunits have four cysteine -rich repeated sequences. Source: Internet
De-aminated alanine, cysteine, glycine, serine, and threonine are converted to pyruvate and can consequently either enter the citric acid cycle as oxaloacetate (an anaplerotic reaction) or as acetyl-CoA to be disposed of as CO 2 and water. Source: Internet
Excluding the few exceptions where methionine may act as a redox sensor (e.g. citation ), methionine residues do not have a catalytic role. citation This is in contrast to cysteine residues, where the thiol group has a catalytic role in many proteins. Source: Internet
Inside the cell, disulfide bridges between cysteine residues within a polypeptide support the protein's tertiary structure. Source: Internet
Biology Selenocysteine has both a lower pKa (5.47) and a lower reduction potential than cysteine. Source: Internet
Disulfide bonds (S-S bonds) between cysteine residues in peptide chains are very important in protein assembly and structure. Source: Internet