Homoserine kinase

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
homoserine kinase
Homoserine kinase tetramer, Methanocaldococcus jannaschii
Identifiers
EC no.2.7.1.39
CAS no.9026-58-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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.

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