Threonine synthase

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threonine synthase
Identifiers
EC number 4.2.3.1
CAS number 9023-97-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

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

O-phospho-L-homoserine + H2O \rightleftharpoons 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.

Structural studies[edit]

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[edit]

  • FLAVIN M, SLAUGHTER C (1960). "Purification and properties of threonine synthetase of Neurospora". J. Biol. Chem. 235: 1103–8. PMID 13823379.