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

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: 1UIM, PDB: 1UIN, PDB: 1V7C, PDB: 1VB3, PDB: 2C2B, PDB: 2C2G, and PDB: 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.


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