In enzymology, a homoserine kinase (EC 2.7.1.39) is an enzyme that catalyzes the chemical reaction
| homoserine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Homoserine kinase tetramer, Methanocaldococcus jannaschii | |||||||||
| Identifiers | |||||||||
| EC no. | 2.7.1.39 | ||||||||
| CAS no. | 9026-58-8 | ||||||||
| 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 | ||||||||
| |||||||||
- ATP + L-homoserine ADP + O-phospho-L-homoserine
Thus, the two substrates of this enzyme are ATP and L-homoserine, whereas its two products are ADP and O-phospho-L-homoserine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:L-homoserine O-phosphotransferase. Other names in common use include homoserine kinase (phosphorylating), and HSK. This enzyme participates in glycine, serine and threonine metabolism.
Structural studies
editAs of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1FWK, 1FWL, 1H72, 1H73, 1H74, and 2PPQ.
References
edit- 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.
- Watanabe Y, Konishi S, Shimura K (1957). "Biosynthesis of threonine from homoserine. VI. Homoserine kinase". J. Biochem. 44 (5): 299–307. doi:10.1093/oxfordjournals.jbchem.a126756.
