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dc.contributor.authorQiu, Yiboen
dc.contributor.authorLian, Yilongen
dc.contributor.authorHemu, Xinyaen
dc.contributor.authorWang, Shujingen
dc.contributor.authorNguyen, Giang Kien Trucen
dc.contributor.authorTam, James Pingkwanen
dc.identifier.citationNguyen, G. K. T., Wang, S., Qiu, Y., Hemu, X., Lian, Y., & Tam, J. P. (2014). Butelase 1 is an Asx-specific ligase enabling peptide macrocyclization and synthesis. Nature Chemical Biology, 10(9), 732-738.en
dc.description.abstractProteases are ubiquitous in nature, whereas naturally occurring peptide ligases, enzymes catalyzing the reverse reactions of proteases, are rare occurrences. Here we describe the discovery of butelase 1, to our knowledge the first asparagine/aspartate (Asx) peptide ligase to be reported. This highly efficient enzyme was isolated from Clitoria ternatea, a cyclic peptide-producing medicinal plant. Butelase 1 shares 71% sequence identity and the same catalytic triad with legumain proteases but does not hydrolyze the protease substrate of legumain. Instead, butelase 1 cyclizes various peptides of plant and animal origin with yields greater than 95%. With Kcat values of up to 17 s(-1) and catalytic efficiencies as high as 542,000 M(-1) s(-1), butelase 1 is the fastest peptide ligase known. Notably, butelase 1 also displays broad specificity for the N-terminal amino acids of the peptide substrate, thus providing a new tool for C terminus-specific intermolecular peptide ligations.en
dc.relation.ispartofseriesNature Chemical Biologyen
dc.rights© 2014 Nature America, Inc. This is the author created version of a work that has been peer reviewed and accepted for publication by Nature Chemical Biology, Nature America, Inc. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [].en
dc.titleButelase 1 is an Asx-specific ligase enabling peptide macrocyclization and synthesisen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
dc.description.versionAccepted versionen
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