Physiological characterization of the ARO10-dependent, broad-substrate-specificity 2-oxo acid decarboxylase activity of Saccharomyces cerevisiae.

@article{Vuralhan2005PhysiologicalCO,
  title={Physiological characterization of the ARO10-dependent, broad-substrate-specificity 2-oxo acid decarboxylase activity of Saccharomyces cerevisiae.},
  author={Zeynep Vuralhan and Marijke A. H. Luttik and Siew Leng Tai and Viktor M. Boer and Marcos A Morais and Dick Schipper and Marinka J. H. Almering and Peter K{\"o}tter and J Richard Dickinson and Jean-Marc Daran and Jack T. Pronk},
  journal={Applied and environmental microbiology},
  year={2005},
  volume={71 6},
  pages={3276-84}
}
Aerobic, glucose-limited chemostat cultures of Saccharomyces cerevisiae CEN.PK113-7D were grown with different nitrogen sources. Cultures grown with phenylalanine, leucine, or methionine as a nitrogen source contained high levels of the corresponding fusel alcohols and organic acids, indicating activity of the Ehrlich pathway. Also, fusel alcohols derived from the other two amino acids were detected in the supernatant, suggesting the involvement of a common enzyme activity. Transcript level… CONTINUE READING
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Inhibition aspects of the bioconversion of phenylalanine to 2-phenylethanol by Saccharomyces cerevisiae

  • D. Stark, D. Zala, T. Munch, B. Sonnleitner, I. W. Marison, U. Von Stockar
  • Enzyme Microbiol
  • 2003
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