Homoserine kinase
homoserine kinase | |||||||||
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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 | ||||||||
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In enzymology, a homoserine kinase (EC 2.7.1.39) is an enzyme that catalyzes the chemical reaction
- 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
[edit]As 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.