Threonine synthase

In enzymology, a threonine synthase (EC number|4.2.3.1) is an enzyme that catalyzes the chemical reaction

:O-phospho-L-homoserine + H₂O $ightleftharpoons$ 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.

tructural 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

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External links

::"The CAS registry number for this enzyme class is CAS registry|9023-97-6."

Gene Ontology (GO) codes