Structure of the penicillin acylase gene from Escherichia coli: a periplasmic enzyme that undergoes multiple proteolytic processing

J Mol Appl Genet. 1985;3(1):36-44.

Abstract

Penicillin acylase is processed from a 90-kD precursor through the cleavage of a leader peptide and two 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.

MeSH terms

  • Amidohydrolases / genetics*
  • Amino Acid Sequence
  • Base Sequence
  • Chromosome Mapping
  • DNA Transposable Elements
  • Escherichia coli / enzymology
  • Escherichia coli / genetics*
  • Genes, Bacterial
  • Immunosorbent Techniques
  • Molecular Weight
  • Penicillin Amidase / genetics*
  • Penicillin Amidase / immunology
  • Penicillin Amidase / metabolism
  • Promoter Regions, Genetic
  • Protein Processing, Post-Translational*

Substances

  • DNA Transposable Elements
  • Amidohydrolases
  • Penicillin Amidase

Associated data

  • GENBANK/M11672
  • GENBANK/M12373