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首页> 外文期刊>Biochemistry >ALDEHYDE DEHYDROGENASE ACTIVITY OF DROSOPHILA MELANOGASTER ALCOHOL DEHYDROGENASE - BURST KINETICS AT HIGH PH AND ALDEHYDE DISMUTASE ACTIVITY AT PHYSIOLOGICAL PH
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ALDEHYDE DEHYDROGENASE ACTIVITY OF DROSOPHILA MELANOGASTER ALCOHOL DEHYDROGENASE - BURST KINETICS AT HIGH PH AND ALDEHYDE DISMUTASE ACTIVITY AT PHYSIOLOGICAL PH

机译：果蝇醛脱氢酶活性的高酸度和醛脱氢酶的生理酸度。

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摘要

The ability of Drosophila alcohol dehydrogenase (D-ADH) to catalyze the oxidation of aldehydes to carboxylic acids has been re-examined. Prior studies are shown to have been compromised by a nonenzymic reaction between the aldehydic substrates and amine-containing buffers, e.g., glycine or Tris, and an amine-catalyzed addition of aldehyde to NAD(+). These reactions interfere with spectrophotometric assays for monitoring aldehyde oxidation and obscure the nature and scope of D-ADH-catalyzed aldehyde oxidation, particularly at physiological pH. Use of nonreactive buffers, such as pyrophosphate or phosphate, and H-1 NMR spectroscopy to monitor all the components of the reaction mixture reveals the facile dismutation of aldehydes into equimolar quantities of the corresponding acids and alcohols at both neutral and high pH. At high pH, dismutation is accompanied by a small burst of NADH production to a steady-state concentration (<10 mu M) that represents a partitioning between NADH dissociation and aldehyde reduction. The increase in A(340) is therefore not a direct measure of the aldehyde oxidation reaction, and the resulting kinetic values cannot be compared to those for alcohol dehydrogenation. The present results for D-ADH, combined with data from the literature, establish that aldehyde oxidation, manifest as dismutation, is a widespread property of alcohol dehydrogenases with potential physiological importance in alcohol metabolism and aldehyde detoxification.
机译：果蝇酒精脱氢酶（D-ADH）催化醛氧化成羧酸的能力已被重新检验。醛类底物与含胺的缓冲液（如甘氨酸或Tris）之间的非酶反应，以及胺催化的醛向NAD（+）的加成反应，都损害了先前的研究。这些反应会干扰用于监测醛氧化的分光光度法，并掩盖了D-ADH催化的醛氧化的性质和范围，特别是在生理pH值下。使用非反应性缓冲剂（例如焦磷酸盐或磷酸盐）和H-1 NMR光谱监测反应混合物的所有组分，可以发现醛在中性和高pH值下容易分解成等摩尔量的相应酸和醇。在高pH下，歧化伴随着NADH产生的小爆发，达到稳态浓度（<10μM），这代表了NADH离解和醛还原之间的分配。因此，A（340）的增加不是醛氧化反应的直接量度，并且所得的动力学值不能与醇脱氢的动力学值进行比较。 D-ADH的当前结果与文献数据相结合，表明醛氧化（表现为歧化）是醇脱氢酶的广泛特性，对酒精代谢和醛解毒具有潜在的生理重要性。

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