STRUCTURE OF THE PENICILLIN ACYLASE GENE FROM ESCHERICHIA-COLI - A PERIPLASMIC ENZYME THAT UNDERGOES MULTIPLE PROTEOLYTIC PROCESSING

  • 1 January 1985
    • journal article
    • research article
    • Vol. 3  (1) , 36-44
Abstract
Penicillin acylase is processed from a 90-kD [kilodalton] precursor through the cleavage of a leader peptide and 2 further endopeptidase cleavages to yield an enzyme that contains a 22-kD (or 23-kD) and a 65-kD subunit. The endopeptidase cleavages require an intact carboxy terminus. This type of processing appears to be unique for a prokaryotic enzyme, having its most closely related analog in the synthesis and processing of preproinsulin and other eukaryotic hormones.