Threonine synthase
Class of enzymes
From Wikipedia, the free encyclopedia
The enzyme threonine synthase (EC 4.2.3.1) catalyzes the chemical reaction
- O-phospho-L-homoserine + H2O L-threonine + phosphate
| threonine synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
threonine synthase dimer, Arabidopsis thaliana | |||||||||
| Identifiers | |||||||||
| EC no. | 4.2.3.1 | ||||||||
| CAS no. | 9023-97-6 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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
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.