Macrocyclization by asparaginyl endopeptidases
© 2017 The Authors. New Phytologist © 2017 New Phytologist Trust.
Publié dans: | The New phytologist. - 1990. - 218(2018), 3 vom: 21. Mai, Seite 923-928 |
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Auteur principal: | |
Autres auteurs: | , |
Format: | Article en ligne |
Langue: | English |
Publié: |
2018
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Accès à la collection: | The New phytologist |
Sujets: | Journal Article Research Support, Non-U.S. Gov't Review asparaginyl endopeptidase (AEP) cyclic peptides macrocycle macrocyclization protease transpeptidation Peptides, Cyclic plus... |
Résumé: | © 2017 The Authors. New Phytologist © 2017 New Phytologist Trust. Contents Summary 923 I. Introduction 923 II. Plant AEPs with macrocyclizing ability 924 III. Mechanism of macrocyclization by AEPs 925 IV. Conclusions 927 Acknowledgements 927 References 927 SUMMARY: Plant asparaginyl endopeptidases (AEPs) are important for the post-translational processing of seed storage proteins via cleavage of precursor proteins. Some AEPs also function as peptide bond-makers during the biosynthesis of several unrelated classes of cyclic peptides, namely the kalata-type cyclic peptides, PawS-Derived Peptides and cyclic knottins. These three families of gene-encoded peptides have different evolutionary origins, but all have recruited AEPs for their maturation. In the last few years, the field has advanced rapidly, with the biochemical characterization of three plant AEPs capable of peptide macrocyclization, and insights have been gained from the first AEP crystal structures, albeit mammalian ones. Although the biochemical studies have improved our understanding of the mechanism of action, the focus now is to understand what changes in AEP sequence and structure enable some plant AEPs to perform macrocyclization reactions |
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Description: | Date Completed 01.10.2019 Date Revised 30.09.2020 published: Print-Electronic CommentIn: New Phytol. 2018 May;218(3):879-881. doi: 10.1111/nph.15156. - PMID 29658638 Citation Status MEDLINE |
ISSN: | 1469-8137 |
DOI: | 10.1111/nph.14511 |