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Alanine dehydrogenase () is an enzyme that catalyzes the chemical reaction :L-alanine + H2O + NAD+ pyruvate + NH3 + NADH + H+ The 3 substrates of this enzyme are L-alanine, water, and nicotinamide adenine dinucleotide+, whereas its 4 products are pyruvate, ammonia, NADH, and hydrogen ion. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-alanine:NAD+ oxidoreductase (deaminating). Other names in common use include AlaDH, L-alanine dehydrogenase, NAD+-linked alanine dehydrogenase, alpha-alanine dehydrogenase, NAD+-dependent alanine dehydrogenase, alanine oxidoreductase, and NADH-dependent alanine dehydrogenase. This enzyme participates in taurine and hypotaurine metabolism and reductive carboxylate cycle ( fixation). ==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「Alanine dehydrogenase」の詳細全文を読む スポンサード リンク
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