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In enzymology, a threonine synthase () is an enzyme that catalyzes the chemical reaction :O-phospho-L-homoserine + H2O L-threonine + phosphate Thus, the two substrates of this enzyme are O-phospho-L-homoserine and H2O, whereas its two products are L-threonine and phosphate. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is O-phospho-L-homoserine phosphate-lyase (adding water L-threonine-forming). Other names in common use include threonine synthetase, and O-phospho-L-homoserine phospho-lyase (adding water). This enzyme participates in glycine, serine and threonine metabolism and vitamin B6 metabolism. It employs one cofactor, pyridoxal phosphate. ==Structural studies== As of late 2007, 7 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「Threonine synthase」の詳細全文を読む スポンサード リンク
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