Make it or break it: Plant AEPs on stage in biotechnology.

Asparaginyl endopeptidase Cyclotide Enzyme Ligase Peptide Transpeptidation

Journal

Biotechnology advances
ISSN: 1873-1899
Titre abrégé: Biotechnol Adv
Pays: England
ID NLM: 8403708

Informations de publication

Date de publication:
12 2020
Historique:
received: 13 07 2020
revised: 02 10 2020
accepted: 20 10 2020
pubmed: 4 11 2020
medline: 2 2 2021
entrez: 3 11 2020
Statut: ppublish

Résumé

Asparaginyl endopeptidases (AEPs) are cysteine proteases that control a myriad of cellular functions in plants, including maturation of seed storage proteins and programmed cell death. Recently, several noteworthy AEPs have been discovered that primarily function as transpeptidases rather than hydrolases, to instead catalyse the formation of new peptide bonds. These AEPs appear to have evolved for the cyclisation of a large class of plant defence peptides called cyclotides. Here we describe recent insights into the structural differences between AEPs that preference peptide ligation over hydrolysis. This knowledge is instrumental for the deployment of AEP ligases as biotechnological tools for in vitro applications such as protein labelling and or cyclization, and for plant molecular farming applications.

Identifiants

pubmed: 33141031
pii: S0734-9750(20)30153-1
doi: 10.1016/j.biotechadv.2020.107651
pii:
doi:

Substances chimiques

Plant Proteins 0
Ligases EC 6.-

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

107651

Informations de copyright

Copyright © 2020. Published by Elsevier Inc.

Auteurs

Mark A Jackson (MA)

Institute for Molecular Bioscience, Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science, The University of Queensland, Brisbane, Queensland 4072, Australia.

Linh T T Nguyen (LTT)

Institute for Molecular Bioscience, Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science, The University of Queensland, Brisbane, Queensland 4072, Australia.

Edward K Gilding (EK)

Institute for Molecular Bioscience, Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science, The University of Queensland, Brisbane, Queensland 4072, Australia.

Thomas Durek (T)

Institute for Molecular Bioscience, Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science, The University of Queensland, Brisbane, Queensland 4072, Australia.

David J Craik (DJ)

Institute for Molecular Bioscience, Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science, The University of Queensland, Brisbane, Queensland 4072, Australia. Electronic address: d.craik@imb.uq.edu.au.

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Classifications MeSH