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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
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Macrocyclization by asparaginyl endopeptidases.

Amy M James1, Joel Haywood1, Joshua S Mylne1

  • 1School of Molecular Sciences & The ARC Centre of Excellence in Plant Energy Biology, The University of Western Australia, 35 Stirling Highway, Crawley, Perth, 6009, Australia.

The New Phytologist
|March 22, 2017
PubMed
Summary
This summary is machine-generated.

Plant asparaginyl endopeptidases (AEPs) process seed proteins and form cyclic peptides. Research is exploring how AEPs

Keywords:
asparaginyl endopeptidase (AEP)cyclic peptidesmacrocyclemacrocyclizationproteasetranspeptidation

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Plant Science

Background:

  • Plant asparaginyl endopeptidases (AEPs) are crucial for post-translational modification of seed storage proteins.
  • Certain AEPs also synthesize cyclic peptides, including kalata-type peptides, PawS-Derived Peptides, and cyclic knottins, despite their diverse evolutionary origins.

Purpose of the Study:

  • To investigate the macrocyclizing ability of plant AEPs.
  • To elucidate the mechanism by which AEPs form peptide bonds for cyclic peptide biosynthesis.
  • To understand the structural and sequence variations in AEPs that confer macrocyclization capabilities.

Main Methods:

  • Biochemical characterization of plant AEPs with macrocyclizing activity.
  • Analysis of crystal structures of AEPs (including mammalian ones) to gain mechanistic insights.
  • Comparative sequence and structural analysis of AEPs involved in macrocyclization.

Main Results:

  • Three plant AEPs capable of peptide macrocyclization have been biochemically characterized.
  • Insights into the mechanism of AEP-mediated macrocyclization have been gained.
  • Mammalian AEP crystal structures provide a basis for understanding plant AEP function.

Conclusions:

  • Plant AEPs play a dual role in protein processing and cyclic peptide synthesis.
  • Recent advancements include the characterization of key AEPs and structural data.
  • Future research will focus on the specific AEP sequence and structural determinants for macrocyclization.