Biosynthetic arginine decarboxylase in Escherichia coli is synthesized as a precursor and located in the cell envelope.

@article{Buch1985BiosyntheticAD,
  title={Biosynthetic arginine decarboxylase in Escherichia coli is synthesized as a precursor and located in the cell envelope.},
  author={J K Buch and Stephen M. Boyle},
  journal={Journal of bacteriology},
  year={1985},
  volume={163 2},
  pages={522-7}
}
The biosynthetic form of arginine decarboxylase (ADC) catalyzes the synthesis of agmatine, a precursor of putrescine, in Escherichia coli. Selective disruption of the cell envelope and an assessment of ADC activity or immunoprecipitable ADC in various fractions demonstrated its location between the cytoplasmic membrane and peptidoglycan layer. Expression in minicells of the speA gene encoding ADC resulted in the production of two immunoprecipitable species (74 and 70 kilodaltons). Studies in… CONTINUE READING