Koivusalo M, Baumann M, Uotila L
Department of Medical Chemistry, University of Helsinki, Finland.
FEBS Lett. 1989 Oct 23;257(1):105-9. doi: 10.1016/0014-5793(89)81797-1.
Formaldehyde dehydrogenase (EC 1.2.1.1) is a widely occurring enzyme which catalyzes the oxidation of S-hydroxymethylglutathione, formed from formaldehyde and glutathione, into S-formyglutathione in the presence of NAD. We determined the amino acid sequences for 5 tryptic peptides (containing altogether 57 amino acids) from electrophoretically homogeneous rat liver formaldehyde dehydrogenase and found that they all were exactly homologous to the sequence of rat liver class III alcohol dehydrogenase (ADH-2). Formaldehyde dehydrogenase was found to be able at high pH values to catalyze the NAD-dependent oxidation of long-chain aliphatic alcohols like n-octanol and 12-hydroxydodecanoate but ethanol was used only at very high substrate concentrations and pyrazole was not inhibitory. The amino acid sequence homology and identical structural and kinetic properties indicate that formaldehyde dehydrogenase and the mammalian class III alcohol dehydrogenases are identical enzymes.
甲醛脱氢酶（EC 1.2.1.1）是一种广泛存在的酶，它在NAD存在的情况下，催化由甲醛和谷胱甘肽形成的S-羟甲基谷胱甘肽氧化为S-甲酰谷胱甘肽。我们测定了来自电泳纯的大鼠肝脏甲醛脱氢酶的5个胰蛋白酶肽段（共含57个氨基酸）的氨基酸序列，发现它们都与大鼠肝脏Ⅲ类醇脱氢酶（ADH-2）的序列完全同源。已发现甲醛脱氢酶在高pH值时能够催化NAD依赖的长链脂肪醇（如正辛醇和12-羟基十二烷酸酯）的氧化，但仅在非常高的底物浓度下才使用乙醇，并且吡唑没有抑制作用。氨基酸序列同源性以及相同的结构和动力学性质表明，甲醛脱氢酶和哺乳动物Ⅲ类醇脱氢酶是相同的酶。
