Proteolytic processing of penicillin amidase from Alcaligenes faecalis cloned in E. coli yields several active forms

@article{Ignatova2004ProteolyticPO,
  title={Proteolytic processing of penicillin amidase from Alcaligenes faecalis cloned in E. coli yields several active forms},
  author={Zoya Ignatova and Stanka Stoeva and Boris Galunsky and Claudia H{\"o}rnle and Allan Nurk and Elke Piotraschke and Wolfgang Voelter and Volker Kasche},
  journal={Biotechnology Letters},
  year={2004},
  volume={20},
  pages={977-982}
}
Of four enzymatically active forms of Alcaligenes faecalis penicillin amidase (EC 3.5.1.11) observed in sonicated cells, two (PA5.5 and PA5.3; subscript denotes pI) could be isolated and purified in two steps from the cells destroyed by osmotic shock. Active enzyme was only found in the periplasm. PA5.5 converts further to PA5.3 which differs in the molecular mass of the A-chain. The origin of these differences is a conversion of the N-terminal Gln to pyrolideno-carboxilic acid and a loss of… CONTINUE READING

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