Threonine synthase
From Wikipedia, the free encyclopedia
In enzymology, a threonine synthase (EC 4.2.3.1) is an enzyme that catalyzes the chemical reaction
- O-phospho-L-homoserine + H2O 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.
Contents |
[edit] 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.
[edit] References
- IUBMB entry for 4.2.3.1
- BRENDA references for 4.2.3.1 (Recommended.)
- PubMed references for 4.2.3.1
- PubMed Central references for 4.2.3.1
- Google Scholar references for 4.2.3.1
- FLAVIN M, SLAUGHTER C (1960). "Purification and properties of threonine synthetase of Neurospora". J. Biol. Chem. 235: 1103–8. PMID 13823379.
[edit] External links
-
- The CAS registry number for this enzyme class is 9023-97-6.