Homoserine kinase (EC 2.7.1.39) is an enzyme that catalyzes the chemical reaction
The enzyme characterised from baker's yeast and Neurospora converts homoserine to O-phospho-L-homoserine by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP). This is part of the biosynthetic pathway to the amino acid, threonine. This enzyme is a transferase, specifically one 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.
Structural studies As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1FWK, PDB: 1FWL, PDB: 1H72, PDB: 1H73, PDB: 1H74, and PDB: 2PPQ.
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