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Threonine synthase

Class of enzymes From Wikipedia, the free encyclopedia

Threonine synthase
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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.

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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

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