From Wikipedia, the free encyclopedia
threonine synthase
threonine synthase dimer, Arabidopsis thaliana
Identifiers
EC no. 4.2.3.1
CAS no. 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 / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

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 1UIM, 1UIN, 1V7C, 1VB3, 2C2B, 2C2G, and 2D1F.

References

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


From Wikipedia, the free encyclopedia
threonine synthase
threonine synthase dimer, Arabidopsis thaliana
Identifiers
EC no. 4.2.3.1
CAS no. 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 / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

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 1UIM, 1UIN, 1V7C, 1VB3, 2C2B, 2C2G, and 2D1F.

References

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



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