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Bacterial aspartic proteinases

J Hill1, L H Phylip

  • 1School of Molecular and Medical Biosciences, University of Wales, Cardiff, UK. HILLJ@Cardiff.ac.uk

FEBS Letters
|June 16, 1997
PubMed
Summary

This study identified the first bacterial aspartic proteinases in Escherichia coli and Haemophilus influenzae. These enzymes cleave synthetic peptides and are inhibited by acetyl-pepstatin, confirming their function.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • Aspartic proteinases are crucial enzymes in vertebrates, fungi, and viruses.
  • Their presence and function in bacteria have not been definitively established.

Purpose of the Study:

  • To investigate the presence and activity of aspartic proteinases in bacteria.
  • To characterize novel bacterial aspartic proteinases.

Main Methods:

  • Polymerase chain reaction (PCR) amplification of DNA regions encoding putative aspartic proteinase domains from Escherichia coli and Haemophilus influenzae.
  • Recombinant protein expression, solubilization, and refolding.
  • Enzyme activity assays using synthetic peptide substrates.
  • Inhibition assays with acetyl-pepstatin.

Main Results:

  • Recombinant proteins from E. coli and H. influenzae were successfully expressed and refolded.
  • Both bacterial proteins exhibited proteolytic activity on synthetic peptide substrates.
  • Enzyme activity was completely inhibited by acetyl-pepstatin, a specific aspartic proteinase inhibitor.

Conclusions:

  • This study provides the first unequivocal evidence for the presence of functional aspartic proteinases in bacteria.
  • Identified bacterial aspartic proteinases share functional similarities with their counterparts in other kingdoms.
  • These findings open new avenues for understanding bacterial enzymology and potential therapeutic targets.

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