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Monomeric human cathepsin E

S D Fowler1, J Kay, B M Dunn

  • 1School of Molecular and Medical Biosciences, University of Wales College of Cardiff, UK.

FEBS Letters
|June 5, 1995
PubMed
Summary
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Human Cathepsin E, a proteinase, normally forms a dimer. Mutating a key cysteine residue created a monomeric form, which retained activity but lost stability at high pH and temperature.

Area of Science:

  • Biochemistry
  • Enzymology
  • Protein Chemistry

Background:

  • Cathepsin E is a aspartic proteinase known to exist as a homodimer.
  • The homodimerization is mediated by an inter-molecular disulphide bond involving a specific cysteine residue near the N-terminus.

Purpose of the Study:

  • To investigate the role of the inter-molecular disulphide bond in Cathepsin E structure and function.
  • To engineer and characterize a monomeric mutant of human Cathepsin E.

Main Methods:

  • Site-directed mutagenesis was used to replace the cysteine residue with alanine.
  • The engineered mutant protein was purified.
  • Enzyme activity was assessed using chromogenic peptide substrates.
  • Enzyme susceptibility to pepstatin inhibition was evaluated.

Related Experiment Videos

  • Protein stability was tested under alkaline pH and elevated temperature conditions.

    • Main Results:

    • A monomeric form of human Cathepsin E was successfully engineered and purified.
    • The monomeric mutant exhibited comparable hydrolytic activity against peptide substrates.
    • Pepstatin inhibition profiles remained similar between the wild-type and mutant enzymes.
    • The monomeric Cathepsin E displayed significantly reduced stability towards alkaline pH and heat.

    Conclusions:

    • The inter-molecular disulphide bond is crucial for the stability of Cathepsin E.
    • While essential for stability, the disulphide bond does not appear to be critical for the catalytic activity or pepstatin inhibition of Cathepsin E.