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Related Experiment Videos

Post-translational peptide bond formation during concanavalin A processing in vitro

P S Sheldon1, J N Keen, D J Bowles

  • 1Centre for Plant Biochemistry, University of Leeds, U.K.

The Biochemical Journal
|December 15, 1996
PubMed
Summary

Post-translational processing converts inactive concanavalin A (Con A) glycoprotein precursors into active lectins. This complex process involves deglycosylation and specific proteolytic cleavage, catalyzed by asparaginyl endopeptidase.

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Endopeptidase activity in jackbeans and its effect on Concanavalin A.

Planta·2013

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Plant Science

Background:

  • Concanavalin A (Con A) is a lectin involved in plant defense and cell recognition.
  • The post-translational modification of Con A is a complex multistep process essential for its biological activity.

Purpose of the Study:

  • To investigate the in vitro processing of the concanavalin A (Con A) glycoprotein precursor.
  • To identify the enzymes and conditions required for Con A maturation.

Main Methods:

  • Utilized 125I-labeled Con A glycoprotein precursor as a substrate for in vitro processing.
  • Employed extracts from immature jackbean cotyledons and purified asparaginyl endopeptidase.
  • Assessed processing activity at various pH levels and analyzed product formation.

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Main Results:

  • Demonstrated that extracts and asparaginyl endopeptidase catalyze Con A processing.
  • Showed the conversion of a 33.5 kDa inactive precursor to an active lectin.
  • Identified optimal processing activity at approximately pH 5.5 and confirmed cleavage at authentic sites.

Conclusions:

  • Asparaginyl endopeptidase is a key enzyme in the post-translational processing of Con A.
  • Con A maturation involves deglycosylation, specific proteolytic cleavage, and de novo peptide bond formation.
  • Understanding Con A processing provides insights into lectin biosynthesis and function.