Ray S, Ray M
Biochim Biophys Acta. 1984 Nov 6;802(1):128-34. doi: 10.1016/0304-4165(84)90042-4.
An enzyme fraction which oxidizes lactaldehyde to lactic acid has been purified from goat liver. This enzyme was found to be identical with the cytosolic aldehyde dehydrogenase. Lactaldehyde was found to be primarily oxidized by this enzyme. Almost 90% of the total lactaldehyde-oxidizing activity is located in the cytosol. Methylglyoxal and glyceraldehyde 3-phosphate were found to be strong competitive inhibitors of this enzyme. Aldehyde dehydrogenase from goat liver mitochondria has also been partially purified and found to be strongly inhibited by these metabolites. The inhibitory effects of these metabolites on both these enzymes are highly pH dependent. The inhibitory effects of both the metabolites have been found to be stronger for the cytosolic enzyme at pH values higher than the physiological pH. For the mitochondrial enzyme, the inhibition with methylglyoxal was more pronounced at higher pH values, whereas stronger inhibition was observed with glyceraldehyde 3-phosphate at physiological pH.
一种能将乳醛氧化为乳酸的酶组分已从山羊肝脏中纯化出来。发现这种酶与胞质醛脱氢酶相同。发现乳醛主要被这种酶氧化。几乎90%的总乳醛氧化活性位于胞质溶胶中。发现甲基乙二醛和3-磷酸甘油醛是这种酶的强竞争性抑制剂。山羊肝脏线粒体中的醛脱氢酶也已部分纯化，并发现受到这些代谢物的强烈抑制。这些代谢物对这两种酶的抑制作用高度依赖于pH值。已发现，在高于生理pH值的情况下，这两种代谢物对胞质酶的抑制作用更强。对于线粒体酶，甲基乙二醛在较高pH值下的抑制作用更明显，而在生理pH值下，3-磷酸甘油醛的抑制作用更强。
