Plant asparaginyl endopeptidases and their structural determinants of function

Samuel G Nonis, Joel Haywood, Joshua S Mylne

Research output: Contribution to journalReview articlepeer-review

4 Citations (Scopus)


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.

Original languageEnglish
Article numberBST20200908
JournalBiochemical Society Transactions
Publication statusE-pub ahead of print - 5 Mar 2021


Dive into the research topics of 'Plant asparaginyl endopeptidases and their structural determinants of function'. Together they form a unique fingerprint.

Cite this