A vinylacetyl isomerase from Clostridium kluyveri.

@article{Bartsch1961AVI,
  title={A vinylacetyl isomerase from Clostridium kluyveri.},
  author={Robert G. Bartsch and H. Albert Barker},
  journal={Archives of biochemistry and biophysics},
  year={1961},
  volume={92},
  pages={
          122-32
        }
}
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14 Citations
Background Citations
2
Methods Citations
3

14 Citations

Citation Type

Citation Type

On the mechanism and some properties of vinylacetyl-CoA delta-isomerase of Clostridium kluyveri.
TLDR
Vinylacetyl-CoA delta-isomerase from Clostridium kluyveri grown on ethanol/acetate was purified 32-fold and the extent of intramolecularity is in agreement with results of experiments conducted in 2H2O with whole cells.
The stereochemistry of vinylacetyl‐CoA‐isomerase of Clostridium kluyveri
Succinate-ethanol fermentation in Clostridium kluyveri: purification and characterisation of 4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA Δ3-Δ2-isomerase
TLDR
The finding of this dehydratase means that all of the enzymes necessary for fermentation of succinate plus ethanol by C. kluyveri have now been demonstrated to exist in this organism and confirms the proposed pathway involving a reduction of succinated via 4-hydroxybutyrate to butyrate.
Studies on the substrate range of Clostridium kluyveri; the use of propanol and succinate
TLDR
A mechanism of succinate metabolism to acetate was proposed which accounts for growth yield, energetics considerations, carbon balances, production of side products and intermediates.
Purification and characterization of a coenzyme-A-dependent succinate-semialdehyde dehydrogenase from Clostridium kluyveri.
TLDR
Cell extracts of Clostridium kluyveri, grown on ethanol plus succinate contained a succinyl-CoA:CoA transferase, a coenzyme-A-dependent succinate-semialdehyde dehydrogenase, and a NAD(+)-dependent 4-hydroxybutyrate dehydrogenases, which suggest a ping-pong mechanism.
Utilization of (E)-2-butenoate (Crotonate) by Clostridium kluyveri and some other Clostridium species
TLDR
Crotonate seems not to be a very special carbon source since C. butyricum and C. pasteurianum grow on crotonate medium supplemented by peptone and yeast extract.
Dehydrogenases involved in the conversion of succinate to 4-hydroxybutanoate by Clostridium kluyveri
TLDR
Data support the hypothesis that C. kluyveri uses succinate as an electron acceptor for the reducing equivalents generated from the ATP-producing oxidation of ethanol.
The enzymic conversion of 3cis- and 3ans-alkenoyl-CoA esters into their 2trans-isomers.
Molecular analysis of the anaerobic succinate degradation pathway in Clostridium kluyveri
TLDR
A region of genomic DNA from Clostridium kluyveri was cloned in Escherichia coli by a screening strategy which was based on heterologous expression of the clostridial 4-hydroxybutyrate dehydrogenase gene, and similarities to the adhE (aad) gene products from E. coli were revealed.
Metabolic properties of Eubacterium pyruvativorans, a ruminal 'hyper-ammonia-producing' anaerobe with metabolic properties analogous to those of Clostridium kluyveri.
TLDR
The fermentative niche of E. pyruvativorans appears to be to scavenge amino acids, lactate and possibly other metabolites in order to generate ATP via acetate formation, using volatile fatty acid elongation with C(2) units derived from other substrates to dispose of reducing equivalents.
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References

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