- Source: Threonine synthase
The enzyme threonine synthase (EC 4.2.3.1) catalyzes the chemical reaction
O-phospho-L-homoserine + H2O
⇌
{\displaystyle \rightleftharpoons }
L-threonine + 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 1UIM, 1UIN, 1V7C, 1VB3, 2C2B, 2C2G, and 2D1F.
References
FLAVIN M, SLAUGHTER C (1960). "Purification and properties of threonine synthetase of Neurospora". J. Biol. Chem. 235 (4): 1103–8. doi:10.1016/S0021-9258(18)69487-6. PMID 13823379.