Threonine synthase

In enzymology, a threonine synthase is an enzyme that catalyzes the chemical reaction


 * O-phospho-L-homoserine + H2O $$\rightleftharpoons$$ L-threonine + phosphate

Thus, the two substrates of this enzyme are O-phospho-L-homoserine and H2O, whereas its two products are L-threonine and phosphate.

This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is O-phospho-L-homoserine phosphate-lyase (adding water L-threonine-forming). Other names in common use include threonine synthetase, and O-phospho-L-homoserine phospho-lyase (adding water). This enzyme participates in glycine, serine and threonine metabolism and vitamin b6 metabolism. It employs one cofactor, pyridoxal phosphate.

Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , and.