threonine synthase
{{Short description|Class of enzymes}}
{{infobox enzyme
| Name = threonine synthase
| EC_number = 4.2.3.1
| CAS_number = 9023-97-6
| GO_code = 0004795
| image = 2c2g.jpg
| width = 270
| caption = threonine synthase dimer, Arabidopsis thaliana
}}
The enzyme threonine synthase (EC 4.2.3.1) catalyzes the chemical reaction
:O-phospho-L-homoserine + H2O 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 {{PDB link|1UIM}}, {{PDB link|1UIN}}, {{PDB link|1V7C}}, {{PDB link|1VB3}}, {{PDB link|2C2B}}, {{PDB link|2C2G}}, and {{PDB link|2D1F}}.
References
{{Reflist}}
- {{cite journal |vauthors=FLAVIN M, SLAUGHTER C | date = 1960 | title = Purification and properties of threonine synthetase of Neurospora | journal = J. Biol. Chem. | volume = 235 | issue = 4 | pages = 1103–8 | doi = 10.1016/S0021-9258(18)69487-6 | doi-access = free | pmid = 13823379 }}
{{Carbon-oxygen lyases}}
{{Enzymes}}
{{Portal bar|Biology|border=no}}
Category:Pyridoxal phosphate enzymes
Category:Enzymes of known structure
{{4.2-enzyme-stub}}