The relative importance of intracellular proteolysis and transport on the yield of the periplasmic enzyme penicillin amidase in Escherichia coli

• Published in: Enzyme and microbial technology Vol. 26; no. 2; pp. 165 - 170
• Main Authors: Ignatova, Z., Enfors, S.-O., Hobbie, M., Taruttis, S., Vogt, C., Kasche, V.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier Inc 01.02.2000; Elsevier Science
• Subjects: acylase; atcc-11105; Biological and medical sciences; Biosynthesis; Biotechnology; Cell membranes; cells; Degradation; E. coli; Enzyme immobilization; Escherichia coli; expression; Fundamental and applied biological sciences. Psychology; Genetic engineering; Genetic technics; invivo; Membrane transport; Methods. Procedures. Technologies; Modification of gene expression level; Penicillin amidase; proteases; protein; Proteolysis; stability; Transport properties; Penicillin amidase; Proteolysis; Membrane transport; E. coli; Molecular processing; Enzyme; Escherichia coli; Bacteria; Hydrolases; Enterobacteriaceae
• ISSN: 0141-0229; 1879-0909; 1879-0909
• DOI: 10.1016/S0141-0229(99)00130-1

Intracellular proteolysis is an important mechanism for regulating the level of the periplasmic enzyme penicillin amidase in Escherichia coli. Evidence is presented that the active enzyme is localized in the periplasmic space and maturation of pro-enzyme occurs during transport through the cytoplasmic membrane or rapidly after its entrance in the periplasm. The rate constants of the transport through cytoplasmic membrane and of the intracellular proteolysis were estimated to be 0.01 h and 0.5 h, respectively. This indicates that more than 90% of the synthesized pre-pro-enzyme is lost by intracellular proteolysis occurring in the cytoplasm.