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In enzymology, a lactaldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction :(S)-lactaldehyde + NAD+ + H2O (S)-lactate + NADH + 2 H+ The 3 substrates of this enzyme are (S)-lactaldehyde, NAD+, and H2O, whereas its 3 products are (S)-lactate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-lactaldehyde:NAD+ oxidoreductase. Other names in common use include L-lactaldehyde:NAD+ oxidoreductase, and nicotinamide adenine dinucleotide (NAD+)-linked dehydrogenase. This enzyme participates in pyruvate metabolism. ==Structural studies== As of late 2007, 4 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「Lactaldehyde dehydrogenase」の詳細全文を読む スポンサード リンク
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