Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/79260
Title: Butelase 1 is an Asx-specific ligase enabling peptide macrocyclization and synthesis
Authors: Qiu, Yibo
Lian, Yilong
Hemu, Xinya
Wang, Shujing
Nguyen, Giang Kien Truc
Tam, James Pingkwan
Issue Date: 2014
Source: Nguyen, 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.
Series/Report no.: Nature Chemical Biology
Abstract: Proteases 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.
URI: https://hdl.handle.net/10356/79260
http://hdl.handle.net/10220/38787
DOI: 10.1038/nchembio.1586
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: [http://dx.doi.org/10.1038/nchembio.1586].
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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