Summary: is the first member of the Enterobacteriaceae found to possess a thiamine pyrophosphate-dependent pyruvate decarboxylase yielding acetaldehyde and CO. In conjunction with an NAD-dependent ethanol dehydrogenase this represents the route of ethanol formation and explains the high ethanol yields previously reported. The organism also possesses an α-acetolactate decarboxylase and is thus able to produce acetoin by both the recognized microbial pathways. Fermentation balances for pyruvate with bacterial suspensions and extracts at pH 6.0 are recorded. NADH oxidase and lactate dehydrogenase are present but NADH-NADP transhydrogenase, coenzyme A-dependent acetaldehyde dehydrogenase, formate dehydrogenase or formate hydrogenlyase could not be detected. The findings are discussed in relation to the classification of and the comparative biochemistry of the Enterobacteriaceae.


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