Noun
a colorless crystalline amino acid found in protein; occurs in the hydrolysates of certain proteins; an essential component of human nutrition
Source: WordNetActivity of MAP kinases is restricted by a number of protein phosphatases, which remove the phosphate groups that are added to specific serine or threonine residues of the kinase and are required to maintain the kinase in an active conformation. Source: Internet
A phosphate group can be attached to the sidechain hydroxyl group of serine, threonine and tyrosine residues, adding a negative charge at that site and producing an unnatural amino acid. 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
Homoserine is the branching point with the threonine pathway, where instead it is isomerised after activating the termainal hydroxyl with phosphate (also used for methionine biosynthesis in plants). Source: Internet
Most of the phosphorylation sites for which such a mobility shift has been described fall in the category of SP and TP sites (i.e. a proline residue follows the phosphorylated serine or threonine residue). Source: Internet
The association of the β rings of the two half-proteasomes triggers threonine -dependent autolysis of the propeptides to expose the active site. Source: Internet