Intramolecular autoproteolysis initiates the maturation of penicillin amidase from Escherichia coli.

@article{Kasche1999IntramolecularAI,
  title={Intramolecular autoproteolysis initiates the maturation of penicillin amidase from Escherichia coli.},
  author={Volker Kasche and Karsten Lummer and A. M. Nurk and Elke Piotraschke and Akker op den Rieks and Stanka Stoeva and Wolfgang Prof Dr Voelter},
  journal={Biochimica et biophysica acta},
  year={1999},
  volume={1433 1-2},
  pages={
          76-86
        }
}
The penicillin amidase (PA) from Escherichia coli belongs to a group of proteolytically processed bacterial enzymes. The mechanism of the maturation of the single polypeptide proenzyme has been studied for the PA from E. coli using a slowly processing mutant proenzyme. The mutant proenzyme was constructed by replacing Thr with Gly in the Thr(263)-Ser(264) bond that must be hydrolysed in active PA. The mutant proenzyme was purified by biospecific affinity chromatography using an immobilized… CONTINUE READING
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