Threonine synthase
In enzymology, a threonine synthase is an enzyme that catalyzes the chemical reaction
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 . Other names in common use include threonine synthetase, and O-phospho-L-homoserine phospho-lyase . This enzyme participates in glycine, serine and threonine metabolism and vitamin B6 metabolism. It employs one cofactor, pyridoxal phosphate.As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes,,,,,, and.
