Homoserine kinase

From Wikipedia, the free encyclopedia

In enzymology, a homoserine kinase (EC 2.7.1.39) is an enzyme that catalyzes the chemical reaction

ATP + L-homoserine $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

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.

[edit] References

IUBMB entry for 2.7.1.39
BRENDA references for 2.7.1.39 (Recommended.)
PubMed references for 2.7.1.39
PubMed Central references for 2.7.1.39
Google Scholar references for 2.7.1.39
FLAVIN M, SLAUGHTER C (1960). "Purification and properties of threonine synthetase of Neurospora". J. Biol. Chem. 235: 1103–8. PMID 13823379.
Watanabe Y, Konishi S and Shimura K (Tokyo). "Biosynthesis of threonine from homoserine. VI. Homoserine kinase". J. Biochem.: 299–307.