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In enzymology, a homoserine kinase () 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== As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and . 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「homoserine kinase」の詳細全文を読む スポンサード リンク
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