Plant asparaginyl endopeptidases and their structural determinants of function

Biochem Soc Trans. 2021 Apr 30;49(2):965-976. doi: 10.1042/BST20200908.


Asparaginyl endopeptidases (AEPs) are versatile enzymes that in biological systems are involved in producing three different catalytic outcomes for proteins, namely (i) routine cleavage by bond hydrolysis, (ii) peptide maturation, including macrocyclisation by a cleavage-coupled intramolecular transpeptidation and (iii) circular permutation involving separate cleavage and transpeptidation reactions resulting in a major reshuffling of protein sequence. AEPs differ in their preference for cleavage or transpeptidation reactions, catalytic efficiency, and preference for asparagine or aspartate target residues. We look at structural analyses of various AEPs that have laid the groundwork for identifying important determinants of AEP function in recent years, with much of the research impetus arising from the potential biotechnological and pharmaceutical applications.

Keywords: peptides; plant proteins; protein structure; proteolysis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Catalytic Domain
  • Cysteine Endopeptidases / chemistry
  • Cysteine Endopeptidases / genetics
  • Cysteine Endopeptidases / metabolism*
  • Hydrolysis
  • Molecular Dynamics Simulation*
  • Peptides / chemistry
  • Peptides / metabolism*
  • Plant Proteins / chemistry
  • Plant Proteins / genetics
  • Plant Proteins / metabolism*
  • Protein Binding
  • Protein Conformation
  • Seed Storage Proteins / chemistry
  • Seed Storage Proteins / genetics
  • Seed Storage Proteins / metabolism*
  • Substrate Specificity


  • Peptides
  • Plant Proteins
  • Seed Storage Proteins
  • Cysteine Endopeptidases
  • asparaginylendopeptidase