Partial purification, characterization and nitrogen regulation of the lysine ɛ-aminotransferase of Streptomyces clavuligerus

@article{Romero1997PartialPC,
  title={Partial purification, characterization and nitrogen regulation of the lysine ɛ-aminotransferase of Streptomyces clavuligerus},
  author={Jorge Romero and Juan F. Martin and Paloma Liras and Arnold L. Demain and N. Rius},
  journal={Journal of Industrial Microbiology and Biotechnology},
  year={1997},
  volume={18},
  pages={241-246}
}
The L-lysine ɛ-aminotransferase (LAT) of Streptomyces clavuligerus was partially purified and characterized. The 51.3-kDa enzyme exhibited optimal activity at pH 7.0–7.5 and 30°C. It catalyzed transfer of the terminal amino group of L-lysine or L-ornithine to α -ketoglutarate. Oxalacetate and pyruvate were also used as acceptors of the amino group but with very low efficiency. Increasing ammonium concentrations added to chemically-defined medium MM enhanced the formation of LAT and decreased… CONTINUE READING

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