Abstract
Publisher Summary Alcohol dehydrogenases catalyze the reversible interconversion of alcohols and aldehydes using NAD(P) as the electron carrier. Such enzymes are present in virtually all life forms and can be divided into three different groups based on their molecular properties, Group l contains the long-chain alcohol dehydrogenases represented by horse liver alcohol dehydrogenase, which is a zinc-containing enzyme, Group II contains short-chain alcohol dehydrogenases, such as the one from Drosophila melanogaster, and these lack metals. Group III contains a small number of iron-dependent alcohol dehydrogenases, which are represented by the second alcohol dehydrogenase, ADH2, purified from Zymomonas mobilis. Several alcohol dehydrogenases have been characterized from hyperthermophilic archaea. A zinc-containing group I enzyme was purified from Sulfolobus solfataricus , and a novel type of iron-containing alcohol dehydrogenase has been purified from Thermococcus litoralis and Thermococcus strain ES-1. This chapter describes the methods used to assay, purify, and characterize the iron-containing alcohol dehydrogenases from T. litoralis and Thermococcus strain ES-1.
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