|
==Introduction== In enzymology, a homoserine dehydrogenase () is an enzyme that catalyzes the chemical reaction :L-homoserine + NAD(P)+ L-aspartate 4-semialdehyde + NAD(P)H + H+ The 2 substrates of this enzyme are L-homoserine and NAD+ (or NADP+), whereas its 3 products are L-aspartate 4-semialdehyde, NADH (or NADPH), and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-homoserine:NAD(P)+ oxidoreductase. Other names in common use include HSDH, and HSD. Homoserine dehydrogenase catalyses the third step in the aspartate pathway; the NAD(P)-dependent reduction of aspartate beta-semialdehyde into homoserine. Homoserine is an intermediate in the biosynthesis of threonine, isoleucine, and methionine. 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 dehydrogenase」の詳細全文を読む スポンサード リンク
|