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Coenzyme specificity of dehydrogenases and fermentation of pyruvate by clostridia.
Arch. Microbiol. 87, 189-202 (1972)
Four clostridial species (C. pasteurianum, C. butylicum, C. butyricum and C. tetanomorphum) grow on pyruvate. Two other species (C. roseum and C. rubrum) only ferment this compound; this is probably due to their inability to synthesize hexose phosphates from pyruvate (fructose-1,6-diphosphatase and pyruvate carboxylase are absent). The fermentation of pyruvate by the above clostridia yields acetate, carbon dioxide, hydrogen and small amounts of compounds more reduced than acetate. Hydrogen pressure increases the amount of ethanol, butanol and butyrate formed during the fermentation of pyruvate. Since C. roseum and C. rubrum contain a ferredoxin: NADP reductase it seems likely that NADPH2 is the coenzyme involved in ethanol formation. In accordance with this acetaldehyde and alcohol dehydrogenases exhibit activity with NADPH2. The glyceraldehyde-3-phosphate dehydrogenase of the clostridia under investigation is NAD specific and so is the β-hydroxy-butyryl-CoA dehydrogenase with the exception of C. kluyveri. The specific activity of hydrogenase and the coenzyme specificity of NAD(P) reductase vary among the clostridial species.
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Publication type
Article: Journal article
Document type
Scientific Article
ISSN (print) / ISBN
0003-9276
e-ISSN
1432-072X
Journal
Archives of Microbiology
Quellenangaben
Volume: 87,
Issue: 3,
Pages: 189-202
Publisher
Springer
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institut für Mikrobiologie