Enzyme Activities Involved in the Metabolism of 1,2-Propanediol by Propionibacterium freudenreichii

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Propionibacterium freudenreichii fermented 1,2-propanediol to yield propionic acid and almost an equimolar amount of n-propanol as end products. A small amount of propionaldehyde and traces of propionyl CoA and propionyl phosphate were detected as intermediates. The propanediol patheway in P. freudenreichii is postulated as follows : The first step is the dehydration from 1,2-propanediol to propionaldehyde by propanediol dehydratase, which requires adenosyl B_<12> as coenzyme. Propionaldehyde is converted into either propionyl CoA or n-propanol by aldehyde dehydrogenase (acylating) or alcohol dehydrogenase, respectively. NADH-linked alcohol dehydrogenase may play a regulatory role in the operation of the pathway. The level of NAD, most of which might be regenerated in the reduction of the aldehyde, adjusted the velocity of the oxidation of the aldehyde.Subsequent oxidation of propionyl CoA to propionic acid was catalized by phosphate acetyltransferase and acetate kinase, and the reduced CoA liberated from propionyl CoA would be turned over to produce the substrate for the aldehyde dehydrogenase.Propanediol dehydratase, aldehyde dehydrogenase (acylating) and alcohol dehydrogenase were induced by the addition of 1,2-propanediol to the culture medium. However, phosphate acetyltransferase and acetate kinase were assumed to be constitutive enzymes operating in the usual pathway of propionic acid fermentation in Propionibacteria.
社団法人日本生物工学会の論文
1978-12-25

Enzyme Activities Involved in the Metabolism of 1,2-Propanediol by Propionibacterium freudenreichii

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