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Homoserine dehydrogenase : ウィキペディア英語版
Homoserine dehydrogenase

==Introduction==
In enzymology, a homoserine dehydrogenase () is an enzyme that catalyzes the chemical reaction
:L-homoserine + NAD(P)+ \rightleftharpoons 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.

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