Jörnvall H, Carlquist M, Jeffery J
Pharmacol Biochem Behav. 1983;18 Suppl 1:67-71. doi: 10.1016/0091-3057(83)90149-1.
"Long" and "short" alcohol dehydrogenases with different structures and catalytic mechanisms exist and the same sub-grouping appears to apply to polyol dehydrogenases. Mammalian liver sorbitol dehydrogenase is clearly related to "long" alcohol dehydrogenases and has structural properties intermediate between those of mammalian and yeast alcohol dehydrogenases. The amino acid sequence of a large segment of the N-terminal part of a liver sorbitol dehydrogenase is now determined and shown to be strictly homologous with the long alcohol dehydrogenases. Seventeen of 93 positions have identical residues among all enzymes compared, defining residues of particular functional significance. Proline and glycine residues suggest largely similar conformations between N-terminal parts of sorbitol dehydrogenase and "long" alcohol dehydrogenases, cysteine and histidine residues suggest a conserved zinc atom at the active site, and other residues correlate with structures of special importance.
具有不同结构和催化机制的“长链”和“短链”乙醇脱氢酶均存在，并且相同的亚分组似乎也适用于多元醇脱氢酶。哺乳动物肝脏山梨醇脱氢酶显然与“长链”乙醇脱氢酶相关，其结构特性介于哺乳动物和酵母乙醇脱氢酶之间。现已确定肝脏山梨醇脱氢酶N端大部分区域的氨基酸序列，结果表明它与长链乙醇脱氢酶具有严格的同源性。在所有比较的酶中，93个位置中有17个位置具有相同的残基，这些残基具有特定的功能意义。脯氨酸和甘氨酸残基表明山梨醇脱氢酶N端部分与“长链”乙醇脱氢酶之间的构象大体相似，半胱氨酸和组氨酸残基表明活性位点存在保守的锌原子，其他残基则与特别重要的结构相关。
