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Title: Peptide asparaginyl ligases—renegade peptide bond makers
Authors: Tam, James P.
Chan, Ning-Yu
Liew, Heng Tai
Tan, Shaun J.
Chen, Yu
Keywords: Science
Issue Date: 2020
Source: Tam, J. P., Chan, N., Liew, H. T., Tan, S. J. & Chen, Y. (2020). Peptide asparaginyl ligases—renegade peptide bond makers. Science China Chemistry, 63(3), 296-307.
Journal: Science China Chemistry
Abstract: Making peptide bonds is tightly controlled by genetic code and machinery which includes cofactors, ATP, and RNAs. In this regard, the stand-alone and genetic-code-independent peptide ligases constitute a new family of renegade peptide-bond makers. A prime example is butelase-1, an Asn/Asp(Asx)-specific ligase that structurally belongs to the asparaginyl endopeptidase family. Butelase-1 specifically recognizes a C-terminal Asx-containing tripeptide motif, Asn/Asp-Xaa-Yaa (Xaa and Yaa are any amino acids), to form a site-specific Asn-Xaa peptide bond either intramolecularly as cyclic proteins or intermolecularly as modified proteins. Our work in the past five years has validated that butelase-1 is a potent and versatile ligase. Here we review the advances in ligases, with a focus on butelase-1, and their applications in engineering bioactive peptides and precision protein modifications, antibody-drug conjugates, and live-cell labeling.
ISSN: 1869-1870
DOI: 10.1007/s11426-019-9648-3
Rights: © 2020 Science in China Press and Springer-Verlag GmbH Germany, part of Springer Nature. All rights reserved. This paper was published in Science China Chemistryand is made available with permission of Science in China Press. The original publication is available at and
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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