Jeffery J, Chesters J, Mills C, Sadler P J, Jörnvall H
EMBO J. 1984 Feb;3(2):357-60. doi: 10.1002/j.1460-2075.1984.tb01811.x.
Evidence is given that tetrameric sorbitol dehydrogenase from sheep liver contains one zinc atom per subunit, most probably located at the active site, and no other specifically bound zinc or iron atom. In alcohol dehydrogenases that are structurally related to sorbitol dehydrogenase, more than one zinc atom per subunit can complicate investigations of zinc atom function. Therefore, sorbitol dehydrogenase will be particularly valuable for defining the precise roles of zinc in alcohol and polyol dehydrogenases, and for establishing correlations of structure and function with other important zinc-containing proteins.
有证据表明,来自羊肝的四聚体山梨醇脱氢酶每个亚基含有一个锌原子,极有可能位于活性位点,且不存在其他特异性结合的锌或铁原子。在结构上与山梨醇脱氢酶相关的醇脱氢酶中,每个亚基不止一个锌原子会使锌原子功能的研究变得复杂。因此,山梨醇脱氢酶对于确定锌在醇脱氢酶和多元醇脱氢酶中的精确作用,以及建立结构与功能与其他重要含锌蛋白质之间的相关性将具有特别重要的价值。