Höög Jan Olov, Strömberg Patrik, Hedberg Jesper J, Griffiths William J
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-17177, Stockholm, Sweden.
Chem Biol Interact. 2003 Feb 1;143-144:175-81. doi: 10.1016/s0009-2797(02)00225-9.
Mammalian alcohol dehydrogenases (ADHs), including ADH1-ADH5/6, interact extensively in the oxidation and reduction of alcohols and aldehydes. ADH1 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.
哺乳动物酒精脱氢酶（ADHs），包括ADH1 - ADH5/6，在醇类和醛类的氧化和还原过程中广泛相互作用。ADH1和ADH2除了参与乙醇氧化外，还涉及多种代谢途径，并且也已被证明参与药物转化。ADH2酶在不同物种间表现出进一步的复杂性，例如在酶学特性方面，啮齿动物的形式基本上缺乏乙醇氧化能力。ADH3（谷胱甘肽依赖性甲醛脱氢酶）已被证明可催化S - 亚硝基谷胱甘肽的还原性分解，表明其参与一氧化氮代谢。质谱分析确定主要酶促产物为谷胱甘肽亚磺酰胺。这种还原性分解直接干扰了已被认为是ADH3生理作用的甲醛清除过程。由于人类ADH5和啮齿动物ADH6行为相似，它们似乎是相应的酶。到目前为止，这些后期的ADHs均未被赋予任何功能。它们可以表达为重组蛋白，但未检测到酶活性。
