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Macrocyclization by asparaginyl endopeptidases
Author(s) -
James Amy M.,
Haywood Joel,
Mylne Joshua S.
Publication year - 2018
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/nph.14511
Subject(s) - cyclic peptide , peptide , cleavage (geology) , peptide sequence , function (biology) , chemistry , posttranslational modification , gene , biochemistry , biology , biosynthesis , computational biology , stereochemistry , genetics , enzyme , paleontology , fracture (geology)
ContentsSummary 923 I. Introduction 923 II. Plant AEPs with macrocyclizing ability 924 III. Mechanism of macrocyclization by AEPs 925 IV. Conclusions 927Acknowledgements 927References 927Summary Plant asparaginyl endopeptidases ( AEP s) are important for the post‐translational processing of seed storage proteins via cleavage of precursor proteins. Some AEP s 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 AEP s for their maturation. In the last few years, the field has advanced rapidly, with the biochemical characterization of three plant AEP s 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 AEP s to perform macrocyclization reactions.