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Recently we described the purification and some properties of a hitherto unknown NADH-dependent enzyme from the Clostridium species La 1 growing on (E)2-butenoate which reduces the carbon-carbon double bond of a&unsaturated carboxylate anions (2-enoates) [ 11. We now report a purified enoate reductase from Clostridium kluyveri and the occurrence of such an activity in the typical amino acid fermenting species Clostridium sporogenes. So far no physiological role of the reductase is known. In the metabolic schemes of clostridia fermenting (E)2-butenoate or ethanol and acetate such an enzyme was not postulated [2]. Up to 1.5% of the soluble protein of the Clostridium sp. La 1 grown under certain conditions consists of the reductase [3,41. In C. sporogenes we found enzyme activities necessary for the following reaction sequence