Purification of glutaryl-CoA dehydrogenase from Pseudomonas sp., an enzyme involved in the anaerobic degradation of benzoate

@article{Hrtel2004PurificationOG,
  title={Purification of glutaryl-CoA dehydrogenase from Pseudomonas sp., an enzyme involved in the anaerobic degradation of benzoate},
  author={U. H{\"a}rtel and E. Eckel and J. Koch and G. Fuchs and D. Linder and W. Buckel},
  journal={Archives of Microbiology},
  year={2004},
  volume={159},
  pages={174-181}
}
Cell-free extracts of Pseudomonas sp. strains KB 740 and K 172 both contained high levels of glutaryl-CoA dehydrogenase when grown anaerobically on benzoate or other aromatic compounds and with nitrate as electron acceptor. [...] Key Result These aromatic compounds have in common benzoyl-CoA as the central aromatic intermediate of anerobic metabolism. The enzymatic activity was almost absent in cells grown aerobically on benzoate regardless whether nitrate was present.Expand
Energetics and biochemistry of fermentative benzoate degradation by Syntrophus gentianae
Anaerobic degradation of aromatic amino acids by the hyperthermophilic archaeon Ferroglobus placidus.
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