The mammalian alcohol dehydrogenases interact in several metabolic pathways
The mammalian alcohol dehydrogenases interact in several metabolic pathways
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DOI：
10.1016/s0009-2797(02)00225-9
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发表时间：
2003-02-01
影响因子：
5.1
通讯作者：
Griffiths, WJ
中科院分区：
文献类型：
--
作者：
Höög, JO;Strömberg, P;Griffiths, WJ
哺乳动物酒精脱氢酶(ADHS)，包括ADH1-ADH5/6，在醇和醛的氧化和还原过程中相互作用广泛。除了乙醇的氧化外，ADHI和ADH2还参与了几种代谢途径，也被证明参与了药物转化。ADH2酶在物种间表现出进一步的复杂性，例如，在啮齿动物形式基本上缺乏乙醇氧化能力的酶特性方面。ADH3(谷胱甘肽依赖的甲醛脱氢酶)可以催化S-亚硝基谷胱甘肽的还原分解，表明它参与了一氧化氮的代谢。质谱仪鉴定了主要的酶产物为谷胱甘肽亚磺酰胺。这种还原分解直接干扰了被认为是ADH3的生理作用的甲醛清除。人的ADH5和啮齿动物的ADH6由于行为相似，似乎是相应的酶。到目前为止，这些后一种ADH都没有被分配给任何职能。它们可以以重组蛋白的形式表达，但没有检测到酶活性。(C)2002爱思唯尔科学爱尔兰有限公司。保留所有权利。
Mammalian alcohol dehydrogenases (ADHs), including ADH1-ADH5/6, interact extensively in the oxidation and reduction of alcohols and aldehydes. ADHI and ADH2 are involved in several metabolic pathways besides the oxidation of ethanol and have also been shown to be involved in drug transformations. The ADH2 enzymes show further complexity among the species, e.g. in enzymatic characteristics where the rodent forms essentially lack ethanol-oxidizing capacity. ADH3 (glutathione-dependent formaldehyde dehydrogenase) has been shown to catalyze the reductive breakdown of S-nitrosoglutathione, indicating involvement in nitric oxide metabolism. Mass spectrometry identified the major enzymatic product as glutathione sulfinamide. This reductive breakdown directly interferes with the formaldehyde scavenging that has been proposed to be the physiological action of ADH3. The human ADH5 and rodent ADH6 seem to be the corresponding enzymes due to their similar behavior. None of these latter ADHs have so far been assigned to any function. They can be expressed as recombinant proteins but no enzymatic activity has been detected. (C) 2002 Elsevier Science Ireland Ltd. All rights reserved.