Homoserine kinase

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homoserine kinase
1fwk.jpg
Homoserine kinase tetramer, Methanocaldococcus jannaschii
Identifiers
EC number2.7.1.39
CAS number9026-58-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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: 1103&ndash, 8. PMID 13823379.
  • Watanabe Y, Konishi S, Shimura K (1957). "Biosynthesis of threonine from homoserine. VI. Homoserine kinase". J. Biochem. 44: 299&ndash, 307.